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Nickel in PDB 6cb7: Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2)

Protein crystallography data

The structure of Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2), PDB code: 6cb7 was solved by Y.Han, B.Zhang, J.Deng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.29 / 1.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.835, 42.835, 147.950, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2) (pdb code 6cb7). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2), PDB code: 6cb7:

Nickel binding site 1 out of 1 in 6cb7

Go back to Nickel Binding Sites List in 6cb7
Nickel binding site 1 out of 1 in the Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Vaccinia Virus A6 N-Terminus (Space Group C2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni201

b:19.3
occ:1.00
N A:HIS0 2.1 13.4 1.0
O A:HIS0 2.2 19.3 1.0
ND1 A:HIS0 2.2 19.5 1.0
O A:HOH404 2.2 23.8 1.0
O A:HOH304 2.2 21.1 1.0
C A:HIS0 2.9 20.7 1.0
CA A:HIS0 2.9 14.6 1.0
CE1 A:HIS0 3.1 22.7 1.0
CG A:HIS0 3.2 16.9 1.0
CB A:HIS0 3.5 15.0 1.0
O A:HOH415 3.9 41.5 1.0
OD1 A:ASP2 4.1 23.0 1.0
N A:MET1 4.2 18.1 1.0
OD2 A:ASP2 4.2 17.9 1.0
NE2 A:HIS0 4.2 22.3 1.0
CD2 A:HIS0 4.3 20.4 1.0
O A:HOH431 4.3 48.1 1.0
CG A:ASP2 4.4 19.2 1.0
CA A:MET1 5.0 15.7 1.0
C A:MET1 5.0 15.6 1.0

Reference:

P.K.Pathak, S.Peng, X.Meng, Y.Han, B.Zhang, F.Zhang, Y.Xiang, J.Deng. Structure of A Lipid-Bound Viral Membrane Assembly Protein Reveals A Modality For Enclosing the Lipid Bilayer. Proc. Natl. Acad. Sci. V. 115 7028 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29915071
DOI: 10.1073/PNAS.1805855115
Page generated: Thu Oct 10 08:21:13 2024

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