Vanadium in PDB 3gp5: Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate

All present enzymatic activity of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate:
5.4.2.1;

The structure of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate, PDB code: 3gp5 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.749, 48.983, 62.960, 105.46, 91.15, 107.42
R / Rfree (%)	17.1 / 23.4

The binding sites of Vanadium atom in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate (pdb code 3gp5). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate, PDB code: 3gp5:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ A:V251 b:17.7 occ:1.00 V A:VO4251 0.0 17.7 1.0 O4 A:VO4251 1.9 17.4 1.0 O2 A:VO4251 1.9 17.1 1.0 O1 A:VO4251 1.9 16.3 1.0 O3 A:3PG252 2.0 19.7 1.0 NE2 A:HIS9 2.3 13.9 1.0 CE1 A:HIS9 3.2 17.0 1.0 CD2 A:HIS9 3.3 14.4 1.0 C2 A:3PG252 3.3 21.2 1.0 OE1 A:GLU87 3.5 14.1 1.0 NH2 A:ARG8 3.9 15.2 1.0 C3 A:3PG252 3.9 21.0 1.0 NE A:ARG60 4.0 14.0 1.0 NE A:ARG8 4.0 15.0 1.0 O A:HOH264 4.1 6.6 1.0 C1 A:3PG252 4.1 19.8 1.0 ND1 A:HIS182 4.1 10.2 1.0 N A:GLY183 4.2 13.8 1.0 NH2 A:ARG60 4.2 14.4 1.0 CD A:GLU87 4.3 15.6 1.0 CB A:HIS182 4.3 11.6 1.0 ND1 A:HIS9 4.4 16.1 1.0 CZ A:ARG8 4.4 15.7 1.0 CG A:HIS9 4.4 14.2 1.0 ND2 A:ASN15 4.5 21.9 1.0 CG A:GLU87 4.5 13.9 1.0 O1 A:3PG252 4.6 21.1 1.0 CA A:HIS182 4.6 12.3 1.0 CZ A:ARG60 4.6 13.4 1.0 CG A:HIS182 4.7 10.8 1.0 O2 A:3PG252 4.7 17.2 1.0 CD A:ARG60 4.9 13.6 1.0 C A:HIS182 4.9 13.7 1.0 OD1 A:ASN15 5.0 23.3 1.0 CB A:GLU87 5.0 14.0 1.0

Vanadium binding site 2 out of 2 in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei with 3-Phosphoglyceric Acid and Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ B:V252 b:19.1 occ:1.00 V B:VO4252 0.0 19.1 1.0 O2 B:VO4252 1.9 17.9 1.0 O3 B:VO4252 1.9 15.5 1.0 O4 B:VO4252 1.9 20.1 1.0 O3 B:3PG253 2.1 21.8 1.0 NE2 B:HIS9 2.2 11.9 1.0 CE1 B:HIS9 3.2 12.1 1.0 CD2 B:HIS9 3.2 12.9 1.0 C2 B:3PG253 3.5 23.2 1.0 OE2 B:GLU87 3.7 15.8 1.0 NH2 B:ARG8 3.7 15.3 1.0 NE B:ARG8 3.9 13.4 1.0 NE B:ARG60 3.9 11.0 1.0 O B:HOH294 4.1 19.7 1.0 N B:GLY183 4.1 16.0 1.0 C3 B:3PG253 4.1 24.4 1.0 ND1 B:HIS182 4.2 17.8 1.0 NH2 B:ARG60 4.3 13.6 1.0 C1 B:3PG253 4.3 20.7 1.0 ND1 B:HIS9 4.3 17.1 1.0 CZ B:ARG8 4.3 16.2 1.0 CG B:HIS9 4.3 15.6 1.0 ND2 B:ASN15 4.4 15.8 1.0 CB B:HIS182 4.4 16.4 1.0 CD B:GLU87 4.5 17.5 1.0 CZ B:ARG60 4.6 12.1 1.0 CA B:HIS182 4.6 15.5 1.0 CG B:GLU87 4.7 17.1 1.0 O2 B:3PG253 4.7 24.4 1.0 CD B:ARG60 4.8 13.3 1.0 CG B:HIS182 4.8 15.7 1.0 C B:HIS182 4.9 15.9 1.0 O1 B:3PG253 4.9 19.3 1.0 CA B:GLY183 4.9 15.5 1.0 OD1 B:ASN15 5.0 21.7 1.0

D.R.Davies, B.L.Staker, J.A.Abendroth, T.E.Edwards, R.Hartley, J.Leonard, H.Kim, A.L.Rychel, S.N.Hewitt, P.J.Myler, L.J.Stewart. An Ensemble of Structures of Burkholderia Pseudomallei 2,3-Bisphosphoglycerate-Dependent Phosphoglycerate Mutase. Acta Crystallogr.,Sect.F V. 67 1044 2011.
ISSN: ESSN 1744-3091
PubMed: 21904048
DOI: 10.1107/S1744309111030405