Vanadium in PDB 6pg0: 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;

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

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 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 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

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