Magnesium in PDB 5koz: Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)

Enzymatic activity of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)

Protein crystallography data

Magnesium Binding Sites:

Magnesium binding site 1 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 1 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:44.6 occ:1.00 OD1 A:ASP194 1.9 42.3 1.0 HO2 A:CAP500 2.0 50.9 1.0 O2 A:CAP500 2.0 42.4 1.0 O7 A:CAP500 2.1 41.5 1.0 OE1 A:GLU195 2.2 47.0 1.0 O2 A:CO3502 2.2 54.2 1.0 O3 A:CAP500 2.4 38.4 1.0 C2 A:CAP500 2.7 43.1 1.0 C A:CAP500 2.7 42.3 1.0 HZ3 A:LYS169 2.9 55.6 1.0 CG A:ASP194 3.0 43.1 1.0 HD21 B:ASN112 3.0 64.6 1.0 HO3 A:CAP500 3.1 46.1 1.0 CD A:GLU195 3.1 49.6 1.0 HZ3 A:LYS167 3.1 48.8 1.0 C3 A:CAP500 3.1 41.4 1.0 HZ1 A:LYS169 3.2 55.6 1.0 H A:GLU195 3.2 53.2 1.0 HZ1 A:LYS167 3.2 48.8 1.0 NZ A:LYS169 3.3 46.3 1.0 HZ2 A:LYS169 3.4 55.6 1.0 C A:CO3502 3.4 54.4 1.0 OE2 A:GLU195 3.4 49.7 1.0 OD2 A:ASP194 3.5 44.1 1.0 HG21 A:ILE165 3.5 45.9 1.0 NZ A:LYS167 3.5 40.6 1.0 HA A:ASP194 3.6 49.6 1.0 HD22 B:ASN112 3.7 64.6 1.0 ND2 B:ASN112 3.7 53.9 1.0 H3 A:CAP500 3.7 49.6 1.0 HZ2 A:LYS167 3.8 48.8 1.0 O1 A:CO3502 3.8 53.7 1.0 O6 A:CAP500 4.0 42.4 1.0 N A:GLU195 4.0 44.4 1.0 C1 A:CAP500 4.1 44.0 1.0 CB A:ASP194 4.2 42.1 1.0 CA A:ASP194 4.3 41.4 1.0 HB3 A:GLU195 4.3 57.8 1.0 NE2 A:HIS288 4.3 48.8 1.0 HG12 A:ILE165 4.3 46.5 1.0 HD3 A:PRO196 4.4 47.0 1.0 C4 A:CAP500 4.4 42.6 1.0 O1 A:CAP500 4.4 44.0 1.0 CG2 A:ILE165 4.5 38.2 1.0 H4 A:CAP500 4.5 51.1 1.0 CG A:GLU195 4.5 49.7 1.0 O3 A:CO3502 4.5 55.0 1.0 HG3 A:LYS169 4.5 53.6 1.0 O B:HOH705 4.6 36.6 1.0 H12 A:CAP500 4.6 52.8 1.0 C A:ASP194 4.7 42.8 1.0 O B:HOH603 4.7 26.7 1.0 HB3 A:ASP194 4.7 50.6 1.0 HE1 A:HIS288 4.7 58.5 1.0 CB A:GLU195 4.8 48.2 1.0 CE A:LYS169 4.8 46.4 1.0 HB2 A:ASP194 4.8 50.6 1.0 CE1 A:HIS288 4.8 48.7 1.0 H11 A:CAP500 4.9 52.8 1.0 HG22 A:ILE165 4.9 45.9 1.0 HG23 A:ILE165 4.9 45.9 1.0 CE A:LYS167 4.9 42.1 1.0 CG B:ASN112 4.9 52.5 1.0 H51 A:CAP500 4.9 51.6 1.0 HE2 A:LYS167 4.9 50.5 1.0 HG3 A:GLU195 5.0 59.6 1.0

Magnesium binding site 2 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 2 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:44.5 occ:1.00 O1 B:CO3502 1.9 43.7 1.0 O3 B:CAP500 1.9 44.4 1.0 OE1 B:GLU195 1.9 43.4 1.0 HO2 B:CAP500 2.0 49.7 1.0 OD1 B:ASP194 2.2 47.1 1.0 O2 B:CAP500 2.3 41.4 1.0 O6 B:CAP500 2.3 46.1 1.0 HO3 B:CAP500 2.6 53.3 1.0 C2 B:CAP500 2.8 43.6 1.0 C3 B:CAP500 2.9 43.2 1.0 C B:CAP500 2.9 45.5 1.0 C B:CO3502 2.9 42.7 1.0 H B:GLU195 3.0 50.2 1.0 HD21 A:ASN112 3.0 48.4 1.0 CD B:GLU195 3.1 42.2 1.0 CG B:ASP194 3.3 47.3 1.0 O2 B:CO3502 3.4 41.9 1.0 HZ3 B:LYS169 3.4 51.0 1.0 H3 B:CAP500 3.4 51.8 1.0 HG21 B:ILE165 3.5 51.7 1.0 HZ2 B:LYS169 3.5 51.0 1.0 HZ1 B:LYS169 3.6 51.0 1.0 HA B:ASP194 3.6 52.4 1.0 OE2 B:GLU195 3.6 42.9 1.0 HZ1 B:LYS167 3.7 50.3 1.0 ND2 A:ASN112 3.7 40.4 1.0 HZ3 B:LYS167 3.7 50.3 1.0 NZ B:LYS169 3.7 42.5 1.0 HD22 A:ASN112 3.7 48.4 1.0 NE2 B:HIS288 3.8 40.6 1.0 HB3 B:GLU195 3.8 49.5 1.0 N B:GLU195 3.9 41.8 1.0 OD2 B:ASP194 4.0 48.6 1.0 O3 B:CO3502 4.0 43.4 1.0 O7 B:CAP500 4.1 46.8 1.0 NZ B:LYS167 4.1 41.9 1.0 C4 B:CAP500 4.1 42.6 1.0 H4 B:CAP500 4.2 51.1 1.0 HG12 B:ILE165 4.2 50.8 1.0 C1 B:CAP500 4.3 44.4 1.0 HE1 B:HIS288 4.3 49.1 1.0 CA B:ASP194 4.3 43.7 1.0 CG B:GLU195 4.3 41.2 1.0 CE1 B:HIS288 4.4 40.9 1.0 H51 B:CAP500 4.4 50.0 1.0 CB B:ASP194 4.4 45.6 1.0 CB B:GLU195 4.4 41.2 1.0 HZ2 B:LYS167 4.5 50.3 1.0 CG2 B:ILE165 4.5 43.1 1.0 HD3 B:PRO196 4.5 58.5 1.0 C B:ASP194 4.6 43.0 1.0 H11 B:CAP500 4.7 53.3 1.0 O1 B:CAP500 4.7 45.6 1.0 C5 B:CAP500 4.7 41.7 1.0 CD2 B:HIS288 4.8 39.9 1.0 CA B:GLU195 4.8 41.4 1.0 HG3 B:GLU195 4.8 49.5 1.0 HG23 B:ILE165 4.8 51.7 1.0 H52 B:CAP500 4.9 50.0 1.0 CG A:ASN112 4.9 40.5 1.0 H12 B:CAP500 4.9 53.3 1.0 HB3 B:ASP194 4.9 54.7 1.0 HG2 B:GLU195 4.9 49.5 1.0 HD2 B:HIS288 5.0 47.9 1.0 HG22 B:ILE165 5.0 51.7 1.0 HG3 B:LYS169 5.0 54.4 1.0

Magnesium binding site 3 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 3 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg501 b:36.0 occ:1.00 OD1 C:ASP194 1.9 34.0 1.0 OE1 C:GLU195 2.0 38.6 1.0 HO2 C:CAP500 2.1 33.9 1.0 O3 C:CO3502 2.2 34.9 1.0 O6 C:CAP500 2.2 31.8 1.0 O2 C:CAP500 2.2 28.3 1.0 O3 C:CAP500 2.4 29.8 1.0 C C:CAP500 2.9 31.0 1.0 C2 C:CAP500 2.9 29.1 1.0 H C:GLU195 2.9 44.8 1.0 HZ3 C:LYS169 3.0 42.6 1.0 HO3 C:CAP500 3.0 35.7 1.0 CG C:ASP194 3.1 35.1 1.0 HD21 D:ASN112 3.1 34.8 1.0 CD C:GLU195 3.1 40.8 1.0 C3 C:CAP500 3.2 28.9 1.0 HZ1 C:LYS169 3.2 42.6 1.0 HZ2 C:LYS169 3.2 42.6 1.0 C C:CO3502 3.3 38.4 1.0 HZ3 C:LYS167 3.3 35.5 1.0 NZ C:LYS169 3.3 35.5 1.0 HZ1 C:LYS167 3.4 35.5 1.0 HA C:ASP194 3.5 39.9 1.0 HG21 C:ILE165 3.5 42.1 1.0 OE2 C:GLU195 3.5 40.4 1.0 HE2 C:HIS288 3.6 44.5 1.0 O2 C:CO3502 3.6 38.6 1.0 HD22 D:ASN112 3.6 34.8 1.0 ND2 D:ASN112 3.7 29.0 1.0 OD2 C:ASP194 3.7 36.8 1.0 H3 C:CAP500 3.8 34.7 1.0 N C:GLU195 3.8 37.3 1.0 NZ C:LYS167 3.8 29.6 1.0 HB3 C:GLU195 3.9 49.9 1.0 O7 C:CAP500 4.1 31.6 1.0 HZ2 C:LYS167 4.2 35.5 1.0 NE2 C:HIS288 4.2 37.1 1.0 CA C:ASP194 4.2 33.2 1.0 CB C:ASP194 4.2 34.3 1.0 HG12 C:ILE165 4.2 42.3 1.0 C1 C:CAP500 4.3 28.7 1.0 CG C:GLU195 4.3 41.6 1.0 HD3 C:PRO196 4.3 47.5 1.0 O1 C:CO3502 4.4 40.0 1.0 CB C:GLU195 4.5 41.5 1.0 CG2 C:ILE165 4.5 35.1 1.0 C4 C:CAP500 4.5 28.7 1.0 C C:ASP194 4.5 35.1 1.0 HG3 C:LYS169 4.5 44.4 1.0 H4 C:CAP500 4.6 34.5 1.0 HE1 C:HIS288 4.6 44.2 1.0 O1 C:CAP500 4.6 29.6 1.0 HB3 C:ASP194 4.7 41.2 1.0 CE1 C:HIS288 4.7 36.8 1.0 CA C:GLU195 4.8 40.5 1.0 O C:HOH649 4.8 23.3 1.0 H12 C:CAP500 4.8 34.4 1.0 H51 C:CAP500 4.8 34.3 1.0 CE C:LYS169 4.8 36.1 1.0 O D:HOH652 4.8 41.1 1.0 HG23 C:ILE165 4.8 42.1 1.0 HB2 C:ASP194 4.9 41.2 1.0 HG2 C:GLU195 4.9 49.9 1.0 HG3 C:GLU195 4.9 49.9 1.0 CG D:ASN112 4.9 27.8 1.0 HG22 C:ILE165 4.9 42.1 1.0

Magnesium binding site 4 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 4 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg501 b:35.6 occ:1.00 OD1 D:ASP194 2.0 37.1 1.0 O3 D:CO3502 2.0 41.9 1.0 HO2 D:CAP500 2.0 42.6 1.0 O6 D:CAP500 2.1 32.1 1.0 O2 D:CAP500 2.1 35.5 1.0 OE1 D:GLU195 2.1 38.2 1.0 O3 D:CAP500 2.3 32.6 1.0 C2 D:CAP500 2.7 32.1 1.0 C D:CAP500 2.7 30.3 1.0 C D:CO3502 2.9 43.0 1.0 HO3 D:CAP500 2.9 39.2 1.0 H D:GLU195 3.1 41.6 1.0 C3 D:CAP500 3.1 31.7 1.0 CG D:ASP194 3.1 35.9 1.0 O2 D:CO3502 3.1 42.8 1.0 HD21 C:ASN112 3.2 39.8 1.0 CD D:GLU195 3.2 38.2 1.0 HZ3 D:LYS169 3.3 48.6 1.0 HG21 D:ILE165 3.3 49.3 1.0 HZ3 D:LYS167 3.3 45.0 1.0 HZ1 D:LYS167 3.4 45.0 1.0 HA D:ASP194 3.5 38.9 1.0 HZ1 D:LYS169 3.5 48.6 1.0 HE2 D:HIS288 3.5 42.3 1.0 HZ2 D:LYS169 3.6 48.6 1.0 NZ D:LYS169 3.6 40.5 1.0 H3 D:CAP500 3.7 38.1 1.0 OE2 D:GLU195 3.7 37.5 1.0 OD2 D:ASP194 3.7 37.4 1.0 ND2 C:ASN112 3.8 33.1 1.0 HD22 C:ASN112 3.8 39.8 1.0 NZ D:LYS167 3.8 37.5 1.0 N D:GLU195 3.9 34.7 1.0 O7 D:CAP500 4.0 29.6 1.0 HG12 D:ILE165 4.0 48.9 1.0 HB3 D:GLU195 4.0 45.6 1.0 O1 D:CO3502 4.1 43.8 1.0 NE2 D:HIS288 4.1 35.3 1.0 C1 D:CAP500 4.2 31.5 1.0 CA D:ASP194 4.2 32.4 1.0 HZ2 D:LYS167 4.2 45.0 1.0 CB D:ASP194 4.2 34.2 1.0 CG2 D:ILE165 4.3 41.1 1.0 C4 D:CAP500 4.3 31.1 1.0 H4 D:CAP500 4.3 37.3 1.0 CG D:GLU195 4.5 38.8 1.0 O1 D:CAP500 4.5 30.9 1.0 HE1 D:HIS288 4.6 42.2 1.0 HD3 D:PRO196 4.6 36.1 1.0 C D:ASP194 4.6 33.0 1.0 CB D:GLU195 4.6 38.0 1.0 H11 D:CAP500 4.6 37.9 1.0 HG23 D:ILE165 4.7 49.3 1.0 CE1 D:HIS288 4.7 35.1 1.0 HB3 D:ASP194 4.8 41.1 1.0 H51 D:CAP500 4.8 36.1 1.0 HG22 D:ILE165 4.8 49.3 1.0 HG3 D:LYS169 4.8 48.5 1.0 CG1 D:ILE165 4.8 40.7 1.0 HD13 D:ILE165 4.8 49.5 1.0 HB2 D:ASP194 4.9 41.1 1.0 H12 D:CAP500 4.9 37.9 1.0 CA D:GLU195 4.9 35.7 1.0 HE2 D:LYS167 5.0 46.0 1.0 O C:HOH621 5.0 35.0 1.0 HB D:ILE165 5.0 48.4 1.0

Magnesium binding site 5 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 5 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg501 b:45.2 occ:1.00 O1 E:CO3502 1.9 42.3 1.0 OE1 E:GLU195 2.0 42.9 1.0 OD1 E:ASP194 2.1 49.9 1.0 HO2 E:CAP500 2.2 53.4 1.0 O7 E:CAP500 2.2 43.7 1.0 O3 E:CAP500 2.3 41.9 1.0 O2 E:CAP500 2.4 44.5 1.0 HO3 E:CAP500 2.9 50.3 1.0 H E:GLU195 2.9 51.5 1.0 C E:CO3502 2.9 39.5 1.0 C E:CAP500 2.9 44.3 1.0 HD21 F:ASN112 3.0 50.8 1.0 C2 E:CAP500 3.0 43.9 1.0 CD E:GLU195 3.1 41.4 1.0 C3 E:CAP500 3.2 42.7 1.0 HE2 E:HIS288 3.2 44.0 1.0 CG E:ASP194 3.3 50.0 1.0 O2 E:CO3502 3.3 37.0 1.0 HZ3 E:LYS169 3.4 51.9 1.0 HG21 E:ILE165 3.4 54.5 1.0 HA E:ASP194 3.5 55.1 1.0 HZ2 E:LYS169 3.6 51.9 1.0 ND2 F:ASN112 3.6 42.3 1.0 OE2 E:GLU195 3.6 41.8 1.0 HZ1 E:LYS169 3.7 51.9 1.0 HB3 E:GLU195 3.7 50.3 1.0 HD22 F:ASN112 3.7 50.8 1.0 HZ3 E:LYS167 3.7 55.9 1.0 N E:GLU195 3.7 42.9 1.0 HZ1 E:LYS167 3.8 55.9 1.0 NZ E:LYS169 3.8 43.3 1.0 H3 E:CAP500 3.8 51.2 1.0 NE2 E:HIS288 3.8 36.6 1.0 OD2 E:ASP194 3.9 51.2 1.0 O3 E:CO3502 4.1 41.9 1.0 O6 E:CAP500 4.1 44.7 1.0 NZ E:LYS167 4.2 46.6 1.0 HG12 E:ILE165 4.2 53.0 1.0 CA E:ASP194 4.2 45.9 1.0 CG E:GLU195 4.3 42.2 1.0 CB E:GLU195 4.3 41.9 1.0 CB E:ASP194 4.3 48.9 1.0 HE1 E:HIS288 4.3 43.6 1.0 CG2 E:ILE165 4.4 45.4 1.0 H4 E:CAP500 4.4 51.2 1.0 CE1 E:HIS288 4.4 36.3 1.0 C4 E:CAP500 4.4 42.6 1.0 C1 E:CAP500 4.4 44.1 1.0 C E:ASP194 4.5 46.4 1.0 HD3 E:PRO196 4.5 45.8 1.0 HZ2 E:LYS167 4.6 55.9 1.0 CA E:GLU195 4.6 40.7 1.0 HG23 E:ILE165 4.7 54.5 1.0 H51 E:CAP500 4.7 49.0 1.0 CD2 E:HIS288 4.8 36.4 1.0 O1 E:CAP500 4.8 44.5 1.0 HG3 E:GLU195 4.8 50.7 1.0 CG F:ASN112 4.8 40.9 1.0 HG3 E:LYS169 4.8 50.6 1.0 HB3 E:ASP194 4.8 58.7 1.0 HG22 E:ILE165 4.9 54.5 1.0 HG2 E:GLU195 4.9 50.7 1.0 H12 E:CAP500 4.9 52.9 1.0 HB2 E:ASP194 5.0 58.7 1.0 HD2 E:HIS288 5.0 43.6 1.0

Magnesium binding site 6 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 6 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg501 b:38.4 occ:1.00 O3 F:CO3502 1.9 35.2 1.0 OD1 F:ASP194 2.0 41.1 1.0 OE1 F:GLU195 2.0 37.6 1.0 HO2 F:CAP500 2.2 47.1 1.0 O7 F:CAP500 2.3 38.3 1.0 O3 F:CAP500 2.3 35.6 1.0 O2 F:CAP500 2.4 39.3 1.0 H F:GLU195 2.8 48.3 1.0 HO3 F:CAP500 2.9 42.7 1.0 C F:CAP500 3.0 38.2 1.0 C2 F:CAP500 3.0 37.8 1.0 C F:CO3502 3.0 36.8 1.0 CD F:GLU195 3.1 39.9 1.0 CG F:ASP194 3.2 43.6 1.0 HD21 E:ASN112 3.2 41.2 1.0 C3 F:CAP500 3.2 36.5 1.0 HG21 F:ILE165 3.3 40.2 1.0 HZ3 F:LYS169 3.3 44.1 1.0 O1 F:CO3502 3.4 35.7 1.0 HA F:ASP194 3.4 51.3 1.0 HZ3 F:LYS167 3.5 53.7 1.0 HZ1 F:LYS167 3.6 53.7 1.0 N F:GLU195 3.7 40.3 1.0 HZ2 F:LYS169 3.7 44.1 1.0 HZ1 F:LYS169 3.7 44.1 1.0 HB3 F:GLU195 3.7 48.2 1.0 OE2 F:GLU195 3.7 39.7 1.0 H3 F:CAP500 3.8 43.8 1.0 NZ F:LYS169 3.8 36.7 1.0 ND2 E:ASN112 3.9 34.3 1.0 HD22 E:ASN112 3.9 41.2 1.0 OD2 F:ASP194 3.9 44.7 1.0 NZ F:LYS167 4.0 44.8 1.0 NE2 F:HIS288 4.0 37.1 1.0 HG12 F:ILE165 4.1 41.5 1.0 CA F:ASP194 4.1 42.8 1.0 O2 F:CO3502 4.2 39.3 1.0 O6 F:CAP500 4.2 37.8 1.0 CB F:ASP194 4.2 43.4 1.0 CG2 F:ILE165 4.3 33.5 1.0 CG F:GLU195 4.3 40.7 1.0 CB F:GLU195 4.3 40.1 1.0 HZ2 F:LYS167 4.3 53.7 1.0 HD3 F:PRO196 4.4 40.9 1.0 HE1 F:HIS288 4.4 45.2 1.0 C1 F:CAP500 4.4 37.3 1.0 C F:ASP194 4.4 41.4 1.0 C4 F:CAP500 4.5 38.0 1.0 CE1 F:HIS288 4.5 37.7 1.0 H4 F:CAP500 4.6 45.6 1.0 HG23 F:ILE165 4.6 40.2 1.0 CA F:GLU195 4.6 39.4 1.0 HB3 F:ASP194 4.7 52.1 1.0 HG22 F:ILE165 4.8 40.2 1.0 HG3 F:LYS169 4.8 45.1 1.0 O1 F:CAP500 4.8 37.0 1.0 H51 F:CAP500 4.8 44.8 1.0 HG3 F:GLU195 4.9 48.9 1.0 H11 F:CAP500 4.9 44.8 1.0 HG2 F:GLU195 4.9 48.9 1.0 CD2 F:HIS288 4.9 37.4 1.0 CG1 F:ILE165 4.9 34.6 1.0 HB2 F:ASP194 4.9 52.1 1.0

Magnesium binding site 7 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 7 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ G:Mg501 b:32.6 occ:1.00 HO2 G:CAP500 1.9 42.4 1.0 O2 G:CO3502 2.0 35.0 1.0 OD1 G:ASP194 2.0 33.8 1.0 O2 G:CAP500 2.1 35.3 1.0 O3 G:CAP500 2.1 33.6 1.0 OE1 G:GLU195 2.1 35.2 1.0 O7 G:CAP500 2.3 33.6 1.0 C2 G:CAP500 2.7 34.3 1.0 HO3 G:CAP500 2.8 40.3 1.0 C G:CAP500 2.8 34.4 1.0 C3 G:CAP500 3.0 32.8 1.0 C G:CO3502 3.0 34.5 1.0 HD21 H:ASN112 3.0 39.3 1.0 H G:GLU195 3.1 37.5 1.0 CG G:ASP194 3.2 32.3 1.0 O1 G:CO3502 3.2 32.2 1.0 CD G:GLU195 3.2 36.0 1.0 HZ3 G:LYS169 3.3 50.5 1.0 HG21 G:ILE165 3.4 37.2 1.0 HZ3 G:LYS167 3.4 39.1 1.0 HZ1 G:LYS169 3.5 50.5 1.0 H3 G:CAP500 3.5 39.4 1.0 HZ1 G:LYS167 3.5 39.1 1.0 HZ2 G:LYS169 3.5 50.5 1.0 HA G:ASP194 3.6 37.8 1.0 NZ G:LYS169 3.6 42.1 1.0 ND2 H:ASN112 3.7 32.8 1.0 OE2 G:GLU195 3.7 35.5 1.0 HD22 H:ASN112 3.7 39.3 1.0 OD2 G:ASP194 3.8 33.4 1.0 NZ G:LYS167 3.9 32.6 1.0 N G:GLU195 3.9 31.2 1.0 HB3 G:GLU195 4.0 42.1 1.0 NE2 G:HIS288 4.1 30.7 1.0 HG12 G:ILE165 4.1 39.1 1.0 O6 G:CAP500 4.1 35.0 1.0 C1 G:CAP500 4.2 34.5 1.0 O3 G:CO3502 4.2 36.9 1.0 HZ2 G:LYS167 4.2 39.1 1.0 C4 G:CAP500 4.2 33.9 1.0 CA G:ASP194 4.3 31.4 1.0 CB G:ASP194 4.3 31.9 1.0 H4 G:CAP500 4.3 40.6 1.0 CG2 G:ILE165 4.4 31.0 1.0 CG G:GLU195 4.5 36.2 1.0 O1 G:CAP500 4.6 35.0 1.0 HD3 G:PRO196 4.6 36.4 1.0 H12 G:CAP500 4.6 41.4 1.0 HE1 G:HIS288 4.6 36.5 1.0 CB G:GLU195 4.6 35.1 1.0 H52 G:CAP500 4.6 40.6 1.0 C G:ASP194 4.6 31.1 1.0 CE1 G:HIS288 4.7 30.4 1.0 HG23 G:ILE165 4.8 37.2 1.0 HB3 G:ASP194 4.8 38.3 1.0 HG3 G:LYS169 4.8 49.7 1.0 H11 G:CAP500 4.9 41.4 1.0 HG22 G:ILE165 4.9 37.2 1.0 CA G:GLU195 4.9 33.0 1.0 CG H:ASN112 4.9 33.8 1.0 CG1 G:ILE165 4.9 32.6 1.0 C5 G:CAP500 4.9 33.8 1.0 O H:HOH701 4.9 29.0 1.0 HB2 G:ASP194 4.9 38.3 1.0 HD13 G:ILE165 5.0 41.6 1.0 CD2 G:HIS288 5.0 30.4 1.0

Magnesium binding site 8 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 8 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ H:Mg501 b:43.6 occ:1.00 OD1 H:ASP194 2.0 39.5 1.0 O1 H:CO3502 2.0 53.2 1.0 HO2 H:CAP500 2.0 49.3 1.0 OE1 H:GLU195 2.1 38.0 1.0 O2 H:CAP500 2.2 41.0 1.0 O6 H:CAP500 2.2 38.3 1.0 O3 H:CAP500 2.2 39.6 1.0 C2 H:CAP500 2.8 40.1 1.0 C H:CAP500 2.8 39.4 1.0 HO3 H:CAP500 2.9 47.6 1.0 H H:GLU195 2.9 37.6 1.0 C3 H:CAP500 3.1 39.5 1.0 C H:CO3502 3.1 62.3 1.0 CG H:ASP194 3.1 38.0 1.0 HD21 G:ASN112 3.2 40.0 1.0 CD H:GLU195 3.2 36.0 1.0 HG21 H:ILE165 3.3 40.6 1.0 HA H:ASP194 3.3 40.2 1.0 HZ3 H:LYS169 3.4 37.0 1.0 O3 H:CO3502 3.4 64.6 1.0 HZ1 H:LYS169 3.5 37.0 1.0 HZ3 H:LYS167 3.5 37.5 1.0 HZ2 H:LYS169 3.5 37.0 1.0 H3 H:CAP500 3.6 47.4 1.0 NZ H:LYS169 3.7 30.9 1.0 OD2 H:ASP194 3.7 39.1 1.0 N H:GLU195 3.7 31.4 1.0 HZ1 H:LYS167 3.7 37.5 1.0 OE2 H:GLU195 3.8 36.0 1.0 ND2 G:ASN112 3.8 33.4 1.0 HD22 G:ASN112 3.8 40.0 1.0 HB3 H:GLU195 3.9 38.7 1.0 NE2 H:HIS288 4.0 38.0 1.0 HG12 H:ILE165 4.1 40.6 1.0 CA H:ASP194 4.1 33.5 1.0 O7 H:CAP500 4.1 39.6 1.0 NZ H:LYS167 4.1 31.2 1.0 CB H:ASP194 4.2 35.2 1.0 O2 H:CO3502 4.2 65.2 1.0 C1 H:CAP500 4.2 40.9 1.0 CG2 H:ILE165 4.3 33.8 1.0 C4 H:CAP500 4.3 39.1 1.0 H4 H:CAP500 4.4 47.0 1.0 CG H:GLU195 4.4 34.1 1.0 C H:ASP194 4.4 33.5 1.0 HE1 H:HIS288 4.5 45.5 1.0 CB H:GLU195 4.5 32.3 1.0 HZ2 H:LYS167 4.5 37.5 1.0 HD3 H:PRO196 4.5 40.4 1.0 CE1 H:HIS288 4.6 37.9 1.0 O1 H:CAP500 4.7 41.0 1.0 HG23 H:ILE165 4.7 40.6 1.0 H11 H:CAP500 4.7 49.1 1.0 H52 H:CAP500 4.7 45.1 1.0 HB3 H:ASP194 4.7 42.2 1.0 CA H:GLU195 4.7 31.1 1.0 HG22 H:ILE165 4.8 40.6 1.0 HB2 H:ASP194 4.8 42.2 1.0 CG1 H:ILE165 4.9 33.9 1.0 HG3 H:LYS169 4.9 38.4 1.0 H12 H:CAP500 4.9 49.1 1.0 HD13 H:ILE165 5.0 41.6 1.0 CD2 H:HIS288 5.0 37.5 1.0 C5 H:CAP500 5.0 37.6 1.0 HB H:ILE165 5.0 41.1 1.0 HG3 H:GLU195 5.0 40.9 1.0

Magnesium binding site 9 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 9 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg501 b:39.5 occ:1.00 O2 I:CO3502 1.9 40.0 1.0 OE1 I:GLU195 1.9 41.5 1.0 OD1 I:ASP194 2.0 35.0 1.0 O6 I:CAP500 2.1 37.1 1.0 HO2 I:CAP500 2.3 44.8 1.0 O3 I:CAP500 2.3 32.8 1.0 O2 I:CAP500 2.4 37.3 1.0 C I:CAP500 2.8 38.0 1.0 HO3 I:CAP500 2.9 39.3 1.0 H I:GLU195 2.9 46.1 1.0 C2 I:CAP500 2.9 36.4 1.0 CD I:GLU195 3.0 44.2 1.0 C I:CO3502 3.0 45.0 1.0 HD21 J:ASN112 3.1 39.5 1.0 C3 I:CAP500 3.2 34.0 1.0 CG I:ASP194 3.2 35.6 1.0 HZ3 I:LYS169 3.2 48.4 1.0 HZ2 I:LYS169 3.3 48.4 1.0 HE2 I:HIS288 3.3 51.0 1.0 HZ1 I:LYS169 3.4 48.4 1.0 OE2 I:GLU195 3.5 44.4 1.0 O3 I:CO3502 3.5 46.1 1.0 HA I:ASP194 3.5 41.9 1.0 NZ I:LYS169 3.5 40.3 1.0 HG21 I:ILE165 3.5 46.8 1.0 HZ3 I:LYS167 3.6 42.1 1.0 HD22 J:ASN112 3.7 39.5 1.0 HZ1 I:LYS167 3.7 42.1 1.0 ND2 J:ASN112 3.7 32.9 1.0 N I:GLU195 3.7 38.4 1.0 H3 I:CAP500 3.7 40.8 1.0 HB3 I:GLU195 3.8 52.0 1.0 OD2 I:ASP194 3.9 36.8 1.0 NE2 I:HIS288 3.9 42.5 1.0 O7 I:CAP500 4.0 38.8 1.0 NZ I:LYS167 4.1 35.1 1.0 O1 I:CO3502 4.1 47.3 1.0 CA I:ASP194 4.2 34.9 1.0 HG12 I:ILE165 4.2 47.4 1.0 CG I:GLU195 4.2 44.3 1.0 CB I:ASP194 4.3 35.4 1.0 HE1 I:HIS288 4.3 51.0 1.0 CB I:GLU195 4.3 43.3 1.0 HD3 I:PRO196 4.3 45.9 1.0 HZ2 I:LYS167 4.4 42.1 1.0 C1 I:CAP500 4.4 36.0 1.0 C4 I:CAP500 4.4 33.6 1.0 CE1 I:HIS288 4.4 42.5 1.0 H4 I:CAP500 4.5 40.4 1.0 C I:ASP194 4.5 35.5 1.0 CG2 I:ILE165 4.5 39.0 1.0 CA I:GLU195 4.7 41.1 1.0 H51 I:CAP500 4.7 40.1 1.0 HB3 I:ASP194 4.7 42.4 1.0 HG3 I:LYS169 4.7 49.8 1.0 HG3 I:GLU195 4.8 53.1 1.0 O1 I:CAP500 4.8 36.6 1.0 HG2 I:GLU195 4.8 53.1 1.0 HG23 I:ILE165 4.8 46.8 1.0 H12 I:CAP500 4.9 43.2 1.0 CD2 I:HIS288 4.9 42.1 1.0 CG J:ASN112 5.0 32.8 1.0 HB2 I:ASP194 5.0 42.4 1.0 HG22 I:ILE165 5.0 46.8 1.0 O J:HOH687 5.0 33.6 1.0 CE I:LYS169 5.0 41.4 1.0 C5 I:CAP500 5.0 33.4 1.0

Magnesium binding site 10 out of 12 in 5koz

Magnesium Binding Sites List in 5koz

Magnesium binding site 10 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound) within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg501 b:44.9 occ:1.00 O2 J:CO3502 1.9 42.6 1.0 OD1 J:ASP194 2.0 40.2 1.0 HO2 J:CAP500 2.0 51.9 1.0 O6 J:CAP500 2.1 41.5 1.0 OE1 J:GLU195 2.1 40.1 1.0 O2 J:CAP500 2.1 43.2 1.0 O3 J:CAP500 2.3 36.0 1.0 C2 J:CAP500 2.8 39.1 1.0 C J:CAP500 2.8 39.0 1.0 HO3 J:CAP500 2.9 43.1 1.0 HD21 I:ASN112 3.0 43.7 1.0 C J:CO3502 3.1 38.3 1.0 H J:GLU195 3.1 40.9 1.0 CG J:ASP194 3.1 36.6 1.0 C3 J:CAP500 3.1 37.6 1.0 HZ3 J:LYS169 3.1 53.2 1.0 CD J:GLU195 3.2 36.1 1.0 HZ1 J:LYS169 3.3 53.2 1.0 HZ3 J:LYS167 3.3 41.8 1.0 HG21 J:ILE165 3.4 40.5 1.0 HZ2 J:LYS169 3.5 53.2 1.0 HZ1 J:LYS167 3.5 41.8 1.0 NZ J:LYS169 3.5 44.3 1.0 HA J:ASP194 3.5 40.6 1.0 HE2 J:HIS288 3.5 42.8 1.0 O3 J:CO3502 3.5 35.1 1.0 OE2 J:GLU195 3.6 36.5 1.0 H3 J:CAP500 3.6 45.1 1.0 OD2 J:ASP194 3.6 37.5 1.0 ND2 I:ASN112 3.7 36.4 1.0 HD22 I:ASN112 3.7 43.7 1.0 NZ J:LYS167 3.8 34.8 1.0 N J:GLU195 3.9 34.0 1.0 O7 J:CAP500 4.0 38.9 1.0 HB3 J:GLU195 4.1 40.5 1.0 NE2 J:HIS288 4.1 35.7 1.0 HZ2 J:LYS167 4.1 41.8 1.0 O1 J:CO3502 4.1 38.9 1.0 HG12 J:ILE165 4.1 42.1 1.0 CA J:ASP194 4.2 33.8 1.0 C1 J:CAP500 4.2 38.5 1.0 CB J:ASP194 4.2 34.4 1.0 C4 J:CAP500 4.3 37.7 1.0 CG2 J:ILE165 4.4 33.7 1.0 H4 J:CAP500 4.4 45.3 1.0 CG J:GLU195 4.5 34.8 1.0 HD3 J:PRO196 4.5 38.0 1.0 HE1 J:HIS288 4.5 43.5 1.0 O1 J:CAP500 4.5 38.2 1.0 C J:ASP194 4.6 34.4 1.0 CB J:GLU195 4.6 33.7 1.0 CE1 J:HIS288 4.6 36.2 1.0 H12 J:CAP500 4.7 46.2 1.0 HG3 J:LYS169 4.7 52.8 1.0 HB3 J:ASP194 4.7 41.2 1.0 HG23 J:ILE165 4.7 40.5 1.0 H52 J:CAP500 4.8 43.2 1.0 HB2 J:ASP194 4.9 41.2 1.0 HG22 J:ILE165 4.9 40.5 1.0 H11 J:CAP500 4.9 46.2 1.0 CA J:GLU195 4.9 32.8 1.0 CG I:ASN112 4.9 37.1 1.0 CE J:LYS169 4.9 45.1 1.0 CG1 J:ILE165 5.0 35.1 1.0 HG3 J:GLU195 5.0 41.7 1.0

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