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Chlorine in PDB 2v1p: Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase

Enzymatic activity of Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase

All present enzymatic activity of Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase:
4.1.99.1;

Protein crystallography data

The structure of Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase, PDB code: 2v1p was solved by A.Kogan, G.Y.Gdalevsky, R.Cohen-Luria, Y.Goldgur, A.H.Parola, O.Almog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.90
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 118.667, 120.200, 171.666, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 22.7

Other elements in 2v1p:

The structure of Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase (pdb code 2v1p). 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 Apo Form of Y74F Mutant E. Coli Tryptophanase, PDB code: 2v1p:

Chlorine binding site 1 out of 1 in 2v1p

Go back to Chlorine Binding Sites List in 2v1p
Chlorine binding site 1 out of 1 in the Crystal Structure of the Apo Form of Y74F Mutant E. Coli Tryptophanase


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 Apo Form of Y74F Mutant E. Coli Tryptophanase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1472

b:32.0
occ:0.50
O A:HOH2132 3.1 15.6 1.0
NE A:ARG69 3.6 16.9 1.0
CB A:ALA65 3.6 15.4 1.0
O A:HOH2029 3.8 54.1 1.0
CD A:ARG69 4.1 17.8 1.0
C A:ALA65 4.5 16.3 1.0
CZ A:ARG69 4.6 19.7 1.0
NH2 A:ARG69 4.7 19.0 1.0
O A:ALA65 4.7 15.7 1.0
CA A:ALA65 4.7 16.7 1.0
N A:ALA66 4.8 15.8 1.0
O A:HOH2065 4.8 30.9 1.0
CG A:ARG69 4.9 14.0 1.0

Reference:

A.Kogan, G.Y.Gdalevsky, R.Cohen-Luria, Y.Goldgur, R.S.Phillips, A.H.Parola, O.Almog. Conformational Changes and Loose Packing Promote E. Coli Tryptophanase Cold Lability. Bmc Struct.Biol. V. 9 65 2009.
ISSN: ESSN 1472-6807
PubMed: 19814824
DOI: 10.1186/1472-6807-9-65
Page generated: Fri Jul 11 00:36:44 2025

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