Magnesium in PDB 4fi4: Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31

The structure of Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31, PDB code: 4fi4 was solved by Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.74 / 2.00
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	137.617, 137.617, 264.696, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 20.4

The structure of Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31 also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Magnesium atom in the Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31 (pdb code 4fi4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31, PDB code: 4fi4:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:27.7 occ:1.00 O A:HOH601 2.0 22.9 1.0 OD2 A:ASP211 2.1 30.0 1.0 OE2 A:GLU237 2.1 25.3 1.0 O A:HOH899 2.1 31.4 1.0 OE1 A:GLU263 2.1 26.9 1.0 O A:HOH898 2.2 36.6 1.0 CD A:GLU263 3.0 24.9 1.0 CG A:ASP211 3.1 29.9 1.0 CD A:GLU237 3.2 28.8 1.0 OE2 A:GLU263 3.2 29.2 1.0 OD1 A:ASP211 3.4 29.8 1.0 NH2 A:ARG284 3.8 23.2 1.0 OE1 A:GLU237 4.0 29.9 1.0 OD2 A:ASP238 4.0 30.3 1.0 O A:HOH603 4.0 27.4 1.0 CD2 A:HIS213 4.0 41.0 1.0 NE2 A:HIS213 4.0 51.1 1.0 O A:HOH602 4.1 24.5 1.0 O A:HOH910 4.1 40.4 1.0 CG A:GLU237 4.1 27.0 1.0 CB A:ASP211 4.4 25.4 1.0 CG A:GLU263 4.4 22.3 1.0 CG A:ASP238 4.7 26.8 1.0 NH1 A:ARG148 4.7 34.6 1.0 CZ A:ARG284 4.8 25.1 1.0 OH A:TYR160 4.8 50.9 1.0 NE A:ARG284 4.8 21.9 1.0 CE2 A:TYR160 4.9 65.3 1.0 CD2 A:HIS313 5.0 22.4 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:29.8 occ:1.00 OE1 B:GLU263 2.0 28.3 1.0 O B:HOH601 2.1 26.9 1.0 OE2 B:GLU237 2.1 25.7 1.0 O B:HOH602 2.1 40.2 1.0 OD2 B:ASP211 2.1 31.9 1.0 O B:HOH603 2.2 29.7 1.0 CD B:GLU263 3.0 27.7 1.0 CG B:ASP211 3.1 41.2 1.0 CD B:GLU237 3.2 32.1 1.0 OE2 B:GLU263 3.2 28.8 1.0 OD1 B:ASP211 3.5 27.1 1.0 NH2 B:ARG284 3.8 28.4 1.0 OD2 B:ASP238 3.9 29.8 1.0 OE1 B:GLU237 4.0 30.1 1.0 CD2 B:HIS213 4.0 43.7 1.0 O B:HOH606 4.0 25.1 1.0 O B:HOH605 4.0 25.5 1.0 CG B:GLU237 4.1 25.6 1.0 O B:HOH604 4.3 32.0 1.0 CG B:GLU263 4.3 26.7 1.0 NE2 B:HIS213 4.3 45.1 1.0 CB B:ASP211 4.4 29.5 1.0 CG B:ASP238 4.6 35.1 1.0 NH1 B:ARG148 4.6 32.8 1.0 OH B:TYR160 4.7 49.6 1.0 CZ B:ARG284 4.7 26.6 1.0 NE B:ARG284 4.8 31.1 1.0 O3 B:GOL502 4.9 54.2 1.0 CD2 B:HIS313 4.9 22.3 1.0 CB B:GLU263 5.0 27.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Mannonate Dehydratase PRK15072 (Target Efi- 502214) From Caulobacter Sp. K31 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg501 b:34.3 occ:1.00 O C:HOH601 2.0 31.9 1.0 OD2 C:ASP211 2.0 35.0 1.0 OE2 C:GLU237 2.1 33.1 1.0 OE1 C:GLU263 2.2 33.4 1.0 O C:HOH602 2.2 36.6 1.0 O C:HOH726 2.3 39.1 1.0 CG C:ASP211 3.0 27.2 1.0 CD C:GLU263 3.1 33.8 1.0 CD C:GLU237 3.1 30.2 1.0 OE2 C:GLU263 3.3 32.9 1.0 OD1 C:ASP211 3.3 30.7 1.0 NH2 C:ARG284 3.8 23.4 1.0 CD2 C:HIS213 3.8 50.4 1.0 OE1 C:GLU237 3.8 29.8 1.0 OD2 C:ASP238 3.9 34.3 1.0 CG C:GLU237 4.0 26.8 1.0 O C:HOH604 4.0 27.5 1.0 NE2 C:HIS213 4.2 60.5 1.0 O C:HOH605 4.2 31.1 1.0 CB C:ASP211 4.3 25.2 1.0 CG C:GLU263 4.4 27.0 1.0 O C:HOH603 4.4 37.4 1.0 CG C:ASP238 4.6 36.1 1.0 NH1 C:ARG148 4.6 35.5 1.0 OH C:TYR160 4.7 52.8 1.0 CZ C:ARG284 4.8 25.4 1.0 NE C:ARG284 4.8 34.3 1.0 CG C:HIS213 5.0 66.0 1.0

Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo. Crystal Structure of Enolase PRK15072 (Target Efi-502214) From Caulobacter Sp. K31 To Be Published.