Magnesium in PDB 1sja: X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine

The structure of X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine, PDB code: 1sja was solved by J.B.Thoden, E.A.Taylor-Ringia, J.B.Garrett, J.A.Gerlt, H.M.Holden, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	215.300, 215.300, 259.100, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine (pdb code 1sja). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine, PDB code: 1sja:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:41.1 occ:1.00 O A:HOH673 2.0 38.3 1.0 O A:AME600 2.1 69.7 1.0 OD2 A:ASP239 2.4 46.0 1.0 OE2 A:GLU214 2.5 59.7 1.0 OD2 A:ASP189 2.5 39.2 1.0 OD1 A:ASP189 3.0 65.6 1.0 C A:AME600 3.0 88.5 1.0 CG A:ASP189 3.1 44.5 1.0 CD A:GLU214 3.2 40.0 1.0 OXT A:AME600 3.3 62.7 1.0 ND2 A:ASN191 3.4 56.8 1.0 CG A:ASP239 3.5 27.0 1.0 OE1 A:GLU240 3.6 53.5 1.0 CB A:ASP239 3.6 28.4 1.0 CG A:GLU214 3.8 47.7 1.0 OE1 A:GLU214 4.0 0.0 1.0 CG A:ASN191 4.0 50.8 1.0 NZ A:LYS263 4.1 55.0 1.0 OD1 A:ASN191 4.2 52.4 1.0 CB A:AME600 4.3 79.4 1.0 CA A:AME600 4.3 0.0 1.0 CB A:ASP189 4.5 20.9 1.0 OD1 A:ASP239 4.6 49.7 1.0 CD A:GLU240 4.6 41.5 1.0 CB A:GLU214 4.6 27.8 1.0 NZ A:LYS163 4.6 33.5 1.0 ND2 A:ASN261 4.8 30.5 1.0 CE2 A:TYR55 4.9 72.1 1.0 CB A:GLN215 4.9 27.4 1.0 CA A:ASN191 4.9 49.8 1.0 CE A:LYS263 5.0 32.0 1.0

Magnesium binding site 2 out of 4 in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:35.5 occ:1.00 O B:AME700 2.0 80.0 1.0 O B:HOH775 2.0 42.4 1.0 OE2 B:GLU214 2.2 33.7 1.0 OD2 B:ASP239 2.3 42.2 1.0 OD2 B:ASP189 2.6 44.4 1.0 CD B:GLU214 3.1 47.0 1.0 C B:AME700 3.2 38.0 1.0 CG B:ASP189 3.3 37.6 1.0 OD1 B:ASP189 3.4 35.7 1.0 CG B:ASP239 3.4 55.1 1.0 ND2 B:ASN191 3.5 79.4 1.0 CB B:ASP239 3.6 29.8 1.0 OXT B:AME700 3.7 80.0 1.0 OE1 B:GLU214 3.7 34.1 1.0 CG B:GLU214 4.0 14.2 1.0 CB B:AME700 4.0 63.0 1.0 OE1 B:GLU240 4.1 42.2 1.0 NZ B:LYS161 4.1 45.1 1.0 NZ B:LYS263 4.2 34.9 1.0 NZ B:LYS163 4.3 57.9 1.0 CA B:AME700 4.3 43.2 1.0 ND2 B:ASN261 4.4 21.5 1.0 CG B:ASN191 4.5 48.9 1.0 CB B:ASP189 4.5 30.5 1.0 OD1 B:ASP239 4.5 39.0 1.0 CE B:LYS263 4.6 36.6 1.0 CB B:GLU214 4.6 65.6 1.0 OD1 B:ASN191 4.8 31.3 1.0 CE2 B:TYR55 4.9 36.5 1.0 CD B:GLU240 4.9 27.0 1.0 CG B:AME700 4.9 54.8 1.0

Magnesium binding site 3 out of 4 in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg801 b:49.5 occ:1.00 O C:AME800 1.7 0.0 1.0 O C:HOH871 2.0 40.4 1.0 OD2 C:ASP189 2.1 41.3 1.0 OD2 C:ASP239 2.4 52.9 1.0 OE2 C:GLU214 2.4 35.6 1.0 C C:AME800 3.0 26.7 1.0 CG C:ASP189 3.0 38.8 1.0 OD1 C:ASP189 3.0 48.1 1.0 CD C:GLU214 3.2 33.4 1.0 CG C:ASP239 3.5 40.3 1.0 ND2 C:ASN191 3.5 38.2 1.0 OXT C:AME800 3.6 0.0 1.0 CB C:ASP239 3.7 51.5 1.0 OE1 C:GLU214 3.8 39.8 1.0 OE1 C:GLU240 4.0 23.5 1.0 CB C:AME800 4.0 75.2 1.0 CG C:GLU214 4.1 35.9 1.0 NZ C:LYS263 4.1 41.9 1.0 CA C:AME800 4.1 97.9 1.0 NZ C:LYS161 4.2 47.7 1.0 CG C:ASN191 4.3 39.5 1.0 CB C:ASP189 4.4 25.8 1.0 NZ C:LYS163 4.4 63.6 1.0 OD1 C:ASN191 4.6 38.8 1.0 CB C:GLU214 4.6 39.6 1.0 OD1 C:ASP239 4.6 60.3 1.0 CE C:LYS263 4.7 29.2 1.0 CD C:GLU240 4.8 26.3 1.0 CE2 C:TYR55 4.8 29.1 1.0 ND2 C:ASN261 4.9 22.2 1.0 OE2 C:GLU240 4.9 29.0 1.0 CE C:LYS161 4.9 31.7 1.0

Magnesium binding site 4 out of 4 in the X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of X-Ray Structure of O-Succinylbenzoate Synthase Complexed with N-Acetylmethionine within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg901 b:54.2 occ:1.00 OXT D:AME900 1.7 83.2 1.0 O D:HOH970 1.9 44.8 1.0 OD2 D:ASP239 2.3 34.0 1.0 OE2 D:GLU214 2.5 42.5 1.0 OD2 D:ASP189 2.6 40.1 1.0 C D:AME900 2.9 61.4 1.0 ND2 D:ASN191 3.3 56.6 1.0 CD D:GLU214 3.3 0.0 1.0 CG D:ASP189 3.3 39.7 1.0 OD1 D:ASP189 3.4 46.0 1.0 CG D:ASP239 3.4 99.9 1.0 CB D:AME900 3.4 40.6 1.0 OE1 D:GLU240 3.6 62.6 1.0 O D:AME900 3.7 72.7 1.0 CB D:ASP239 3.7 65.9 1.0 CA D:AME900 3.8 0.0 1.0 CG D:GLU214 3.8 30.9 1.0 NZ D:LYS263 4.0 50.5 1.0 CG D:ASN191 4.0 0.0 1.0 OE1 D:GLU214 4.1 41.4 1.0 OD1 D:ASN191 4.2 54.2 1.0 CD D:GLU240 4.4 54.7 1.0 OD1 D:ASP239 4.5 37.0 1.0 NZ D:LYS161 4.5 32.3 1.0 CE2 D:TYR55 4.7 69.1 1.0 OE2 D:GLU240 4.7 58.9 1.0 CB D:ASP189 4.7 22.4 1.0 CG D:AME900 4.8 91.6 1.0 N D:AME900 4.9 0.0 1.0 CB D:GLU214 4.9 41.0 1.0

J.B.Thoden, E.A.Taylor-Ringia, J.B.Garrett, J.A.Gerlt, H.M.Holden, I.Rayment. Evolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous O-Succinylbenzoate Synthase From Amycolatopsis Biochemistry V. 43 5716 2004.
ISSN: ISSN 0006-2960
PubMed: 15134446
DOI: 10.1021/BI0497897