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Chlorine in PDB 6ocf: The Crystal Structure of VASH1-Svbp Complex

Enzymatic activity of The Crystal Structure of VASH1-Svbp Complex

All present enzymatic activity of The Crystal Structure of VASH1-Svbp Complex:
3.4.17.17;

Protein crystallography data

The structure of The Crystal Structure of VASH1-Svbp Complex, PDB code: 6ocf was solved by F.Li, X.Luo, H.Yu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.21 / 2.10
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 100.558, 100.558, 206.730, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of VASH1-Svbp Complex (pdb code 6ocf). 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 The Crystal Structure of VASH1-Svbp Complex, PDB code: 6ocf:

Chlorine binding site 1 out of 1 in 6ocf

Go back to Chlorine Binding Sites List in 6ocf
Chlorine binding site 1 out of 1 in the The Crystal Structure of VASH1-Svbp Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of VASH1-Svbp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:75.8
occ:1.00
NH2 A:ARG130 2.5 38.7 0.4
CZ A:ARG130 3.5 39.8 0.4
NE A:ARG130 3.9 40.9 0.4
O A:GLU123 4.1 35.6 1.0
CG A:GLN126 4.3 22.7 1.0
NH2 A:ARG127 4.3 83.3 1.0
N A:ARG127 4.5 28.0 1.0
CB A:GLN126 4.5 24.3 1.0
CE2 A:TYR228 4.6 32.1 1.0
CD2 A:TYR228 4.6 28.8 1.0
NH1 A:ARG130 4.6 39.6 0.4
NE A:ARG130 4.8 40.4 0.6
CA A:ARG127 4.8 35.0 1.0
CB A:ARG127 4.8 47.5 1.0
CZ A:TYR228 4.8 35.7 1.0
CG A:TYR228 4.8 28.6 1.0
CZ A:ARG127 4.9 84.3 1.0
CD A:ARG130 4.9 39.1 0.6
C A:GLN126 4.9 30.4 1.0
C A:GLU123 5.0 31.1 1.0
CA A:GLU123 5.0 28.4 1.0

Reference:

F.Li, Y.Hu, S.Qi, X.Luo, H.Yu. Structural Basis of Tubulin Detyrosination By Vasohibins. Nat.Struct.Mol.Biol. V. 26 583 2019.
ISSN: ESSN 1545-9985
PubMed: 31235910
DOI: 10.1038/S41594-019-0242-X
Page generated: Sat Jul 12 17:48:38 2025

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