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Tungsten in PDB 1ohd: Structure of CDC14 in Complex with Tungstate

Protein crystallography data

The structure of Structure of CDC14 in Complex with Tungstate, PDB code: 1ohd was solved by C.H.Gray, V.M.Good, N.K.Tonks, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.66 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.750, 51.950, 64.998, 90.00, 118.57, 90.00
R / Rfree (%) 22.6 / 28.7

Tungsten Binding Sites:

The binding sites of Tungsten atom in the Structure of CDC14 in Complex with Tungstate (pdb code 1ohd). 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 Structure of CDC14 in Complex with Tungstate, PDB code: 1ohd:

Tungsten binding site 1 out of 1 in 1ohd

Go back to Tungsten Binding Sites List in 1ohd
Tungsten binding site 1 out of 1 in the Structure of CDC14 in Complex with Tungstate


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Structure of CDC14 in Complex with Tungstate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:W1380

b:49.8
occ:1.00
W A:WO41380 0.0 49.8 1.0
O1 A:WO41380 1.6 48.2 1.0
O4 A:WO41380 1.6 44.4 1.0
O3 A:WO41380 1.6 52.3 1.0
O2 A:WO41380 1.6 48.2 1.0
SG A:CYS314 3.5 36.1 1.0
N A:GLY319 3.7 37.1 1.0
N A:ALA316 4.0 43.7 1.0
OD1 A:ASP287 4.1 59.4 1.0
CA A:GLY319 4.1 37.0 1.0
NH2 A:ARG320 4.2 30.1 1.0
N A:ARG320 4.2 37.0 1.0
CB A:ALA316 4.3 43.1 1.0
NE A:ARG320 4.3 31.8 1.0
CB A:CYS314 4.4 40.2 1.0
N A:LEU318 4.4 40.3 1.0
N A:LYS315 4.5 41.2 1.0
N A:GLY317 4.5 42.4 1.0
CA A:ALA316 4.6 43.3 1.0
C A:GLY319 4.7 37.8 1.0
CZ A:ARG320 4.7 30.9 1.0
C A:LEU318 4.7 38.4 1.0
CB A:LYS315 4.8 44.7 1.0
CA A:LEU318 4.9 39.0 1.0
C A:ALA316 4.9 41.9 1.0
CB A:LEU318 5.0 38.5 1.0
CA A:LYS315 5.0 42.9 1.0

Reference:

C.H.Gray, V.M.Good, N.K.Tonks, D.Barford. The Structure of the Cell Cycle Protein CDC14 Reveals A Proline-Directed Protein Phosphatase Embo J. V. 22 3524 2003.
ISSN: ISSN 0261-4189
PubMed: 12853468
DOI: 10.1093/EMBOJ/CDG348
Page generated: Wed Dec 16 02:33:13 2020

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