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Chlorine in PDB 4gr4: Crystal Structure of SLGN1DELTAASUB

Protein crystallography data

The structure of Crystal Structure of SLGN1DELTAASUB, PDB code: 4gr4 was solved by D.A.Herbst, G.Zocher, T.Stehle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.72 / 2.44
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 88.110, 148.610, 109.580, 90.00, 113.34, 90.00
R / Rfree (%) 18 / 21.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of SLGN1DELTAASUB (pdb code 4gr4). 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 SLGN1DELTAASUB, PDB code: 4gr4:

Chlorine binding site 1 out of 1 in 4gr4

Go back to Chlorine Binding Sites List in 4gr4
Chlorine binding site 1 out of 1 in the Crystal Structure of SLGN1DELTAASUB


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 SLGN1DELTAASUB within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl501

b:58.6
occ:1.00
O B:HOH652 3.2 33.7 1.0
N B:ARG443 3.3 32.6 1.0
NH2 B:ARG443 3.6 39.3 1.0
CA B:GLU442 3.7 41.5 1.0
CB B:GLU442 3.8 42.5 1.0
C B:GLU442 4.0 40.8 1.0
NH1 B:ARG21 4.0 0.6 1.0
CG B:GLU442 4.0 47.1 1.0
OE2 B:GLU442 4.1 57.5 1.0
CA B:ARG443 4.3 31.4 1.0
O B:ARG443 4.3 34.1 1.0
CD B:ARG443 4.4 46.1 1.0
CB B:ARG443 4.4 30.8 1.0
CD1 B:LEU416 4.5 27.5 1.0
CD B:GLU442 4.6 59.2 1.0
CZ B:ARG443 4.7 51.9 1.0
C B:ARG443 4.8 34.5 1.0
CZ B:ARG21 4.9 0.4 1.0
O B:GLY441 4.9 53.8 1.0
CG B:ARG443 4.9 40.2 1.0
NE B:ARG443 5.0 46.6 1.0

Reference:

D.A.Herbst, B.Boll, G.Zocher, T.Stehle, L.Heide. Structural Basis of the Interaction of Mbth-Like Proteins, Putative Regulators of Nonribosomal Peptide Biosynthesis, with Adenylating Enzymes. J.Biol.Chem. V. 288 1991 2013.
ISSN: ISSN 0021-9258
PubMed: 23192349
DOI: 10.1074/JBC.M112.420182
Page generated: Sat Dec 12 10:40:30 2020

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