Atomistry » Vanadium » PDB 1b8j-1yv3 » 1e59
Atomistry »
  Vanadium »
    PDB 1b8j-1yv3 »
      1e59 »

Vanadium in PDB 1e59: E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate

Enzymatic activity of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate

All present enzymatic activity of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate:
5.4.2.1;

Protein crystallography data

The structure of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate, PDB code: 1e59 was solved by C.S.Bond, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 61.249, 112.142, 40.948, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 21.3

Other elements in 1e59:

The structure of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate (pdb code 1e59). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 4 binding sites of Vanadium where determined in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate, PDB code: 1e59:
Jump to Vanadium binding site number: 1; 2; 3; 4;

Vanadium binding site 1 out of 4 in 1e59

Go back to Vanadium Binding Sites List in 1e59
Vanadium binding site 1 out of 4 in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1001

b:19.2
occ:0.50
V1 A:VO31001 0.0 19.2 0.5
O1 A:VO31001 1.7 37.9 0.5
O30 A:VO31001 1.8 51.8 0.5
O0 A:VO31001 1.8 40.0 0.0
O3 A:VO31001 1.8 20.8 1.0
V2 A:VO31001 3.3 12.4 1.0
O00 A:VO31001 3.3 30.4 0.5
O A:HOH2114 3.7 13.4 1.0
O A:HOH2009 3.8 19.3 1.0
O A:HOH2263 3.9 24.0 1.0
ND2 A:ASN16 3.9 27.5 1.0
O A:HOH2262 4.0 28.0 1.0
O2 A:VO31001 4.0 17.1 1.0
O6 A:VO31001 4.2 17.1 1.0
O A:HOH2209 4.2 12.1 1.0
O A:HOH2115 4.2 16.9 1.0
NH2 A:ARG9 4.4 14.4 1.0
O4 A:VO31001 4.6 12.8 1.0
O A:HOH2006 4.7 18.8 1.0
CB A:ASN16 4.7 22.8 1.0
V4 A:VO31001 4.7 38.9 0.5
OG1 A:THR22 4.8 12.5 1.0
CG A:ASN16 4.8 26.7 1.0

Vanadium binding site 2 out of 4 in 1e59

Go back to Vanadium Binding Sites List in 1e59
Vanadium binding site 2 out of 4 in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1001

b:12.4
occ:1.00
V2 A:VO31001 0.0 12.4 1.0
O2 A:VO31001 1.7 17.1 1.0
O4 A:VO31001 1.7 12.8 1.0
O3 A:VO31001 1.8 20.8 1.0
O6 A:VO31001 1.8 17.1 1.0
V1 A:VO31001 3.3 19.2 0.5
V3 A:VO31001 3.5 14.7 1.0
O30 A:VO31001 3.8 51.8 0.5
O A:HOH2115 3.9 16.9 1.0
O A:HOH2116 3.9 11.1 1.0
N A:THR22 3.9 8.1 1.0
CE2 A:TYR91 4.0 10.4 1.0
O A:HOH2114 4.1 13.4 1.0
O5 A:VO31001 4.1 13.8 1.0
CB A:THR22 4.1 9.9 1.0
NZ A:LYS99 4.2 19.2 1.0
O0 A:VO31001 4.2 40.0 0.0
N A:GLY23 4.3 9.4 1.0
CD2 A:TYR91 4.3 10.1 1.0
OE2 A:GLU88 4.4 10.1 1.0
O1 A:VO31001 4.4 37.9 0.5
OG1 A:THR22 4.4 12.5 1.0
O7 A:VO31001 4.5 13.4 1.0
CA A:THR22 4.5 8.6 1.0
O8 A:VO31001 4.6 9.4 0.5
O00 A:VO31001 4.7 30.4 0.5
O A:HOH2262 4.7 28.0 1.0
CD A:GLU88 4.8 7.4 1.0
CG A:GLU88 4.8 7.7 1.0
CE A:LYS99 4.9 14.5 1.0
C A:THR22 4.9 9.2 1.0
C A:PHE21 4.9 10.1 1.0

Vanadium binding site 3 out of 4 in 1e59

Go back to Vanadium Binding Sites List in 1e59
Vanadium binding site 3 out of 4 in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 3 of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1001

b:14.7
occ:1.00
V3 A:VO31001 0.0 14.7 1.0
O7 A:VO31001 1.7 13.4 1.0
O5 A:VO31001 1.7 13.8 1.0
O8 A:VO31001 1.7 9.4 0.5
O6 A:VO31001 1.8 17.1 1.0
V4 A:VO31001 3.4 38.9 0.5
V2 A:VO31001 3.5 12.4 1.0
OH A:TYR91 3.6 12.7 1.0
O A:HOH2115 3.7 16.9 1.0
CE2 A:TYR91 3.9 10.4 1.0
NZ A:LYS99 3.9 19.2 1.0
NH2 A:ARG115 4.0 36.8 1.0
NH1 A:ARG116 4.0 14.8 1.0
ND2 A:ASN185 4.0 9.0 1.0
O2 A:VO31001 4.0 17.1 1.0
O00 A:VO31001 4.1 30.4 0.5
CZ A:TYR91 4.2 11.6 1.0
NH2 A:ARG116 4.2 20.1 1.0
O11 A:VO31001 4.2 40.0 0.0
NE A:ARG115 4.3 20.9 1.0
O A:HOH2116 4.3 11.1 1.0
O10 A:VO31001 4.4 40.0 0.0
O A:HOH2210 4.5 16.8 1.0
O4 A:VO31001 4.5 12.8 1.0
O3 A:VO31001 4.5 20.8 1.0
CZ A:ARG115 4.5 28.3 1.0
CZ A:ARG116 4.6 13.4 1.0
NH2 A:ARG89 4.6 11.9 1.0
CE A:LYS99 4.9 14.5 1.0

Vanadium binding site 4 out of 4 in 1e59

Go back to Vanadium Binding Sites List in 1e59
Vanadium binding site 4 out of 4 in the E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 4 of E.Coli Cofactor-Dependent Phosphoglycerate Mutase Complexed with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1001

b:38.9
occ:0.50
V4 A:VO31001 0.0 38.9 0.5
O10 A:VO31001 1.6 40.0 0.0
O11 A:VO31001 1.7 40.0 0.0
O00 A:VO31001 1.8 30.4 0.5
O8 A:VO31001 1.8 9.4 0.5
V3 A:VO31001 3.4 14.7 1.0
O0 A:VO31001 3.5 40.0 0.0
NH2 A:ARG9 3.7 14.4 1.0
NH2 A:ARG115 3.7 36.8 1.0
O A:HOH2115 3.8 16.9 1.0
NH2 A:ARG116 3.9 20.1 1.0
O A:HOH2210 4.1 16.8 1.0
O6 A:VO31001 4.1 17.1 1.0
O A:HOH2264 4.1 21.1 1.0
O5 A:VO31001 4.2 13.8 1.0
O7 A:VO31001 4.6 13.4 1.0
OD1 A:ASN206 4.7 29.6 1.0
NZ A:LYS99 4.7 19.2 1.0
V1 A:VO31001 4.7 19.2 0.5
CZ A:ARG9 4.8 11.9 1.0
O30 A:VO31001 4.9 51.8 0.5
NH1 A:ARG9 4.9 16.4 1.0
CZ A:ARG115 5.0 28.3 1.0

Reference:

C.S.Bond, M.White, W.N.Hunter. Mechanistic Implications For Escherichia Coli Cofactor-Dependent Phosphoglycerate Mutase Based on the High-Resolution Crystal Structure of A Vanadate Complex. J.Mol.Biol. V. 316 1071 2002.
ISSN: ISSN 0022-2836
PubMed: 11884145
DOI: 10.1006/JMBI.2002.5418
Page generated: Thu Oct 29 07:04:12 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy