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Tungsten in PDB 2i6m: Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate

Enzymatic activity of Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate

All present enzymatic activity of Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate, PDB code: 2i6m was solved by H.M.Chu, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 72.288, 72.288, 32.518, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 23.3

Tungsten Binding Sites:

The binding sites of Tungsten atom in the Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate (pdb code 2i6m). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate, PDB code: 2i6m:

Tungsten binding site 1 out of 1 in 2i6m

Go back to Tungsten Binding Sites List in 2i6m
Tungsten binding site 1 out of 1 in the Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Crystal Structure of the Complexes of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Tungstate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:W1380

b:50.2
occ:0.40
W A:WO41380 0.0 50.2 0.4
O1 A:WO41380 1.6 50.0 0.4
O4 A:WO41380 1.6 49.3 0.4
O3 A:WO41380 1.6 49.3 0.4
O2 A:WO41380 1.6 49.9 0.4
OD1 A:ASP69 3.5 35.8 1.0
O A:HOH5226 3.6 27.1 1.0
O A:HOH5224 3.8 17.7 1.0
N A:GLY98 3.9 18.2 1.0
SG A:CYS96 4.0 23.6 1.0
N A:GLY101 4.0 19.8 1.0
NH2 A:ARG102 4.1 18.9 1.0
NE A:ARG102 4.3 16.2 1.0
CA A:GLY98 4.4 17.9 1.0
N A:ILE100 4.6 19.1 1.0
CA A:GLY101 4.6 18.5 1.0
N A:ARG102 4.6 15.8 1.0
N A:GLY99 4.6 18.1 1.0
CG A:ASP69 4.6 30.6 1.0
CZ A:ARG102 4.7 18.1 1.0
O A:HOH5227 4.8 28.2 1.0
CB A:VAL97 4.8 17.5 1.0
N A:VAL97 4.8 17.1 1.0
C A:GLY98 4.9 19.3 1.0

Reference:

H.M.Chu, A.H.J.Wang. Enzyme-Substrate Interactions Revealed By the Crystal Structures of the Archaeal Sulfolobus Ptp-Fold Phosphatase and Its Phosphopeptide Complexes Proteins V. 66 996 2006.
ISSN: ISSN 0887-3585
PubMed: 17173287
DOI: 10.1002/PROT.21262
Page generated: Wed Dec 16 02:34:34 2020

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