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Vanadium in PDB 6pg0: Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State

Enzymatic activity of Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State

All present enzymatic activity of Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State, PDB code: 6pg0 was solved by D.S.Cui, J.M.Lipchock, J.P.Loria, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.80 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.227, 88.227, 104.068, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 22.5

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State (pdb code 6pg0). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State, PDB code: 6pg0:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 6pg0

Go back to Vanadium Binding Sites List in 6pg0
Vanadium binding site 1 out of 2 in the Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V301

b:30.3
occ:1.00
V A:VO4301 0.0 30.3 1.0
O3 A:VO4301 1.9 30.4 1.0
O1 A:VO4301 1.9 32.4 1.0
O4 A:VO4301 1.9 27.3 1.0
O2 A:VO4301 1.9 30.0 1.0
SG A:CYS215 3.0 27.1 1.0
O A:HOH423 3.3 48.9 1.0
OE1 A:GLN262 3.4 33.0 1.0
OD1 A:ASP181 3.6 29.9 0.8
O A:HOH487 3.7 28.1 1.0
N A:GLY220 3.8 25.3 1.0
CB A:CYS215 3.9 23.9 1.0
N A:ALA217 3.9 23.1 1.0
NE A:ARG221 4.0 27.5 1.0
NH2 A:ARG221 4.1 25.3 1.0
N A:ARG221 4.1 23.9 1.0
CA A:GLY220 4.2 23.7 1.0
CB A:ALA217 4.2 26.9 1.0
N A:SER216 4.2 22.6 1.0
N A:GLY218 4.2 23.3 1.0
O1 A:GOL305 4.4 40.2 1.0
N A:ILE219 4.4 24.3 1.0
CD A:GLN262 4.4 32.2 1.0
CA A:ALA217 4.5 23.5 1.0
CG A:ASP181 4.5 33.0 0.8
CZ A:ARG221 4.6 26.2 1.0
C A:GLY220 4.7 24.9 1.0
NE2 A:GLN262 4.8 31.5 1.0
C A:ALA217 4.8 25.1 1.0
OD2 A:ASP181 4.9 34.8 0.8
C A:ILE219 4.9 24.8 1.0
C A:SER216 4.9 25.1 1.0
CG1 A:ILE219 4.9 22.7 1.0
CA A:SER216 5.0 24.2 1.0
CG A:ARG221 5.0 24.3 1.0
CB A:SER216 5.0 25.7 1.0
CB A:ARG221 5.0 21.4 1.0

Vanadium binding site 2 out of 2 in 6pg0

Go back to Vanadium Binding Sites List in 6pg0
Vanadium binding site 2 out of 2 in the Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Protein Tyrosine Phosphatase 1B (1-301), P188A Mutant, Vanadate Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V302

b:72.8
occ:1.00
V A:VO4302 0.0 72.8 1.0
O2 A:VO4302 1.9 43.2 1.0
O1 A:VO4302 1.9 29.5 1.0
O4 A:VO4302 1.9 58.6 1.0
O3 A:VO4302 1.9 50.7 1.0
O A:HOH407 2.3 43.0 1.0
O A:HIS54 3.7 25.7 1.0
O A:HOH547 4.3 44.9 1.0
ND1 A:HIS54 4.3 27.6 1.0
C A:HIS54 4.7 29.2 1.0
CB A:HIS54 4.7 24.5 1.0
CG A:HIS54 5.0 27.6 1.0

Reference:

D.S.Cui, J.M.Lipchock, D.Brookner, J.P.Loria. Uncovering the Molecular Interactions in the Catalytic Loop That Modulate the Conformational Dynamics in Protein Tyrosine Phosphatase 1B. J.Am.Chem.Soc. V. 141 12634 2019.
ISSN: ESSN 1520-5126
PubMed: 31339043
DOI: 10.1021/JACS.9B04470
Page generated: Wed Dec 16 02:31:57 2020

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