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Chlorine in PDB 3qq7: Crystal Structure of the P97 N-Terminal Domain

Protein crystallography data

The structure of Crystal Structure of the P97 N-Terminal Domain, PDB code: 3qq7 was solved by P.Haenzelmann, H.Schindelin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.28 / 2.65
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 60.560, 60.560, 63.110, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 23.6

Other elements in 3qq7:

The structure of Crystal Structure of the P97 N-Terminal Domain also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the P97 N-Terminal Domain (pdb code 3qq7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the P97 N-Terminal Domain, PDB code: 3qq7:

Chlorine binding site 1 out of 1 in 3qq7

Go back to Chlorine Binding Sites List in 3qq7
Chlorine binding site 1 out of 1 in the Crystal Structure of the P97 N-Terminal Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the P97 N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:83.9
occ:1.00
NH2 A:ARG113 3.2 0.5 1.0
CB A:HIS115 3.2 82.6 1.0
CO A:CO402 3.5 0.3 1.0
CG A:HIS115 3.7 98.9 1.0
ND1 A:HIS115 3.7 0.6 1.0
CZ A:ARG113 3.8 0.1 1.0
NE A:ARG113 3.9 0.2 1.0
CB A:HIS183 4.0 72.6 0.5
CA A:HIS115 4.0 73.2 1.0
CB A:HIS183 4.2 72.0 0.5
ND1 A:HIS183 4.2 76.6 0.5
N A:HIS115 4.3 65.8 1.0
O A:ILE114 4.3 71.7 1.0
CG A:HIS183 4.5 77.4 0.5
C A:ILE114 4.5 65.1 1.0
ND1 A:HIS183 4.5 82.1 0.5
CG A:HIS183 4.5 74.6 0.5
CD2 A:HIS115 4.7 0.0 1.0
CE1 A:HIS115 4.7 0.1 1.0
OE2 A:GLU167 4.8 0.2 1.0
NH1 A:ARG113 4.9 0.8 1.0

Reference:

P.Hanzelmann, A.Buchberger, H.Schindelin. Hierarchical Binding of Cofactors to the Aaa Atpase P97. Structure V. 19 833 2011.
ISSN: ISSN 0969-2126
PubMed: 21645854
DOI: 10.1016/J.STR.2011.03.018
Page generated: Sat Dec 12 10:05:11 2020

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