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Vanadium in PDB 6pm8: Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State

Enzymatic activity of Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State

All present enzymatic activity of Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State, PDB code: 6pm8 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) 33.66 / 2.06
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.298, 88.298, 104.003, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 22

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State (pdb code 6pm8). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Protein Tyrosine Phosphatase 1B (1-301), P180A Mutant, Vanadate Bound State, PDB code: 6pm8:

Vanadium binding site 1 out of 1 in 6pm8

Go back to Vanadium Binding Sites List in 6pm8
Vanadium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B (1-301), P180A 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), P180A Mutant, Vanadate Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V301

b:38.8
occ:0.76
V A:VO4301 0.0 38.8 0.8
O4 A:VO4301 1.9 27.2 0.8
O2 A:VO4301 1.9 39.5 0.8
O1 A:VO4301 1.9 40.7 0.8
O3 A:VO4301 1.9 31.3 0.8
NE2 A:GLN262 3.1 25.7 0.5
SG A:CYS215 3.2 33.8 1.0
OD1 A:ASP181 3.3 40.7 0.5
HO1 A:GOL304 3.3 65.5 1.0
O A:HOH406 3.4 57.0 1.0
O A:HOH443 3.4 33.8 1.0
N A:GLY220 3.7 28.3 1.0
O1 A:GOL304 3.7 54.6 1.0
N A:ALA217 4.0 23.6 1.0
CA A:GLY220 4.1 25.6 1.0
NH2 A:ARG221 4.2 28.1 1.0
CB A:ALA217 4.2 31.1 1.0
CD A:GLN262 4.2 35.4 0.5
NE A:ARG221 4.2 27.7 1.0
N A:ARG221 4.2 23.4 1.0
CB A:CYS215 4.3 19.8 1.0
CG A:ASP181 4.3 39.8 0.5
N A:GLY218 4.3 25.3 1.0
N A:ILE219 4.4 25.0 1.0
N A:SER216 4.5 22.9 1.0
OD2 A:ASP181 4.6 46.0 0.5
CA A:ALA217 4.6 26.9 1.0
CZ A:ARG221 4.7 28.3 1.0
OE1 A:GLN262 4.7 33.3 0.5
CG1 A:ILE219 4.7 24.1 1.0
C A:GLY220 4.7 23.8 1.0
H11 A:GOL304 4.8 63.4 1.0
C A:ILE219 4.9 24.5 1.0
C1 A:GOL304 4.9 52.8 1.0
C A:ALA217 4.9 25.4 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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