Atomistry » Vanadium » PDB 1z12-3myh » 3i80
Atomistry »
  Vanadium »
    PDB 1z12-3myh »
      3i80 »

Vanadium in PDB 3i80: Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step

Enzymatic activity of Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step

All present enzymatic activity of Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step:
3.1.3.48;

Protein crystallography data

The structure of Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step, PDB code: 3i80 was solved by T.A.S.Brandao, S.J.Johnson, A.C.Hengge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.71 / 2.25
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 87.840, 87.840, 103.790, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 23.5

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step (pdb code 3i80). 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 - Transition State Analog For the Second Catalytic Step, PDB code: 3i80:

Vanadium binding site 1 out of 1 in 3i80

Go back to Vanadium Binding Sites List in 3i80
Vanadium binding site 1 out of 1 in the Protein Tyrosine Phosphatase 1B - Transition State Analog For the Second Catalytic Step


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 - Transition State Analog For the Second Catalytic Step within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V322

b:38.2
occ:1.00
V A:VO4322 0.0 38.2 1.0
O1 A:VO4322 1.9 35.2 1.0
O3 A:VO4322 1.9 36.7 1.0
O2 A:VO4322 1.9 36.0 1.0
O4 A:VO4322 2.1 39.1 1.0
SG A:CYS215 2.5 31.7 1.0
CB A:CYS215 3.5 27.0 1.0
O A:HOH490 3.8 40.5 1.0
N A:GLY220 3.8 35.7 1.0
OE1 A:GLN262 3.8 35.9 1.0
N A:ALA217 3.9 27.7 1.0
OD2 A:ASP181 3.9 43.8 1.0
NE A:ARG221 3.9 34.6 1.0
NH2 A:ARG221 3.9 30.1 1.0
O A:HOH497 4.0 48.1 1.0
N A:ARG221 4.0 27.9 1.0
N A:SER216 4.0 30.8 1.0
N A:GLY218 4.1 33.6 1.0
CA A:GLY220 4.2 32.6 1.0
CB A:ALA217 4.3 30.0 1.0
N A:ILE219 4.3 31.9 1.0
O1 A:GOL326 4.4 64.6 1.0
CZ A:ARG221 4.4 33.8 1.0
CA A:ALA217 4.5 31.8 1.0
C A:GLY220 4.7 34.5 1.0
CA A:CYS215 4.7 27.6 1.0
CD A:GLN262 4.7 30.8 1.0
C A:ALA217 4.8 33.1 1.0
CA A:SER216 4.8 30.2 1.0
C A:CYS215 4.8 26.1 1.0
CB A:ARG221 4.8 29.2 1.0
CG A:ASP181 4.8 49.6 1.0
C A:SER216 4.8 28.6 1.0
CB A:SER216 4.9 30.1 1.0
CG A:ARG221 4.9 28.6 1.0
C A:ILE219 4.9 32.8 1.0
CA A:GLY218 4.9 32.5 1.0
CD A:ARG221 5.0 27.6 1.0

Reference:

T.A.Brandao, A.C.Hengge, S.J.Johnson. Insights Into the Reaction of Protein-Tyrosine Phosphatase 1B: Crystal Structures For Transition State Analogs of Both Catalytic Steps. J.Biol.Chem. V. 285 15874 2010.
ISSN: ISSN 0021-9258
PubMed: 20236928
DOI: 10.1074/JBC.M109.066951
Page generated: Fri Oct 11 19:20:14 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy