Atomistry » Chlorine » PDB 5vmt-5vus » 5vn5
Atomistry »
  Chlorine »
    PDB 5vmt-5vus »
      5vn5 »

Chlorine in PDB 5vn5: Crystal Structure of Ligy From Sphingobium Sp. Strain Syk-6

Protein crystallography data

The structure of Crystal Structure of Ligy From Sphingobium Sp. Strain Syk-6, PDB code: 5vn5 was solved by E.Kuatsjah, A.C.K.Chan, M.J.Kobylarz, M.E.P.Murphy, L.D.Eltis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.61 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 60.020, 195.361, 178.249, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 18.9

Other elements in 5vn5:

The structure of Crystal Structure of Ligy From Sphingobium Sp. Strain Syk-6 also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ligy From Sphingobium Sp. Strain Syk-6 (pdb code 5vn5). 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 Ligy From Sphingobium Sp. Strain Syk-6, PDB code: 5vn5:

Chlorine binding site 1 out of 1 in 5vn5

Go back to Chlorine Binding Sites List in 5vn5
Chlorine binding site 1 out of 1 in the Crystal Structure of Ligy From Sphingobium Sp. Strain Syk-6


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 Ligy From Sphingobium Sp. Strain Syk-6 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl410

b:30.0
occ:1.00
ZN C:ZN400 1.9 24.4 1.0
HG3 C:GLU282 2.4 40.4 1.0
HE1 C:HIS223 3.1 29.4 1.0
NE2 C:HIS179 3.1 19.8 1.0
CG C:GLU282 3.2 33.7 1.0
NE2 C:HIS8 3.2 24.1 1.0
HE1 C:HIS179 3.3 23.2 1.0
NE2 C:HIS223 3.3 23.8 1.0
NE2 C:HIS6 3.4 24.8 1.0
HE2 C:PHE194 3.4 27.1 1.0
CD C:GLU282 3.5 37.3 1.0
HG2 C:GLU282 3.5 40.4 1.0
CE1 C:HIS223 3.5 24.5 1.0
HD2 C:HIS8 3.5 29.9 1.0
O C:HOH524 3.6 32.7 1.0
CE1 C:HIS179 3.6 19.3 1.0
CD2 C:HIS8 3.8 24.9 1.0
OE2 C:GLU282 3.8 38.8 1.0
CE2 C:PHE194 3.9 22.6 1.0
OE1 C:GLU282 3.9 38.9 1.0
HD2 C:PHE194 4.1 26.6 1.0
CE1 C:HIS6 4.2 24.2 1.0
CD2 C:PHE194 4.2 22.1 1.0
HE1 C:HIS6 4.3 29.1 1.0
CD2 C:HIS6 4.3 24.9 1.0
CD2 C:HIS179 4.4 20.0 1.0
HD2 C:HIS6 4.4 29.9 1.0
CE1 C:HIS8 4.4 23.9 1.0
HB2 C:GLU282 4.4 36.1 1.0
CB C:GLU282 4.5 30.1 1.0
HD2 C:PRO73 4.6 24.3 1.0
HG2 C:PRO73 4.6 23.1 1.0
CD2 C:HIS223 4.7 25.1 1.0
CZ C:PHE194 4.7 20.4 1.0
HE1 C:HIS8 4.7 28.7 1.0
HD2 C:HIS179 4.7 24.0 1.0
HG23 C:VAL286 4.8 46.3 1.0
ND1 C:HIS223 4.8 24.4 1.0
HZ C:PHE194 4.8 24.5 1.0
ND1 C:HIS179 4.9 17.9 1.0
HB3 C:GLU282 4.9 36.1 1.0
HG11 C:VAL258 4.9 28.2 1.0
HG21 C:VAL286 5.0 46.3 1.0

Reference:

E.Kuatsjah, A.C.K.Chan, M.J.Kobylarz, M.E.P.Murphy, L.D.Eltis. The Bacterialmeta-Cleavage Hydrolase Ligy Belongs to the Amidohydrolase Superfamily, Not to the Alpha / Beta-Hydrolase Superfamily. J. Biol. Chem. V. 292 18290 2017.
ISSN: ESSN 1083-351X
PubMed: 28935670
DOI: 10.1074/JBC.M117.797696
Page generated: Sat Jul 12 09:57:36 2025

Last articles

K in 9F90
K in 9ES6
K in 9EWD
K in 9ETN
K in 9ESI
K in 9ESH
K in 9ES4
K in 9ES5
K in 9ES2
K in 9ES0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy