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Chlorine in PDB 6esd: Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum

Enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum

All present enzymatic activity of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum:
1.4.3.23;

Protein crystallography data

The structure of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 6esd was solved by H.E.Lai, M.Morgan, S.Moore, P.Freemont, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.78 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 151.610, 172.600, 94.670, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum (pdb code 6esd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 6esd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6esd

Go back to Chlorine Binding Sites List in 6esd
Chlorine binding site 1 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum


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 L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:69.4
occ:1.00
NH1 B:ARG64 2.6 54.5 1.0
OH B:TYR309 3.4 50.9 1.0
N5 B:FAD501 3.7 50.9 1.0
CZ B:ARG64 3.8 43.8 1.0
C4X B:FAD501 3.9 45.6 1.0
NE2 B:HIS163 4.0 48.9 1.0
CD2 B:HIS163 4.2 46.8 1.0
C4 B:FAD501 4.2 45.9 1.0
C5X B:FAD501 4.3 50.6 1.0
O4 B:FAD501 4.3 41.7 1.0
CZ B:TYR309 4.4 52.1 1.0
CH2 B:TRP397 4.4 48.8 1.0
CE2 B:TYR309 4.4 45.8 1.0
NE B:ARG64 4.4 45.1 1.0
CZ3 B:TRP397 4.6 41.0 1.0
CZ2 B:TRP397 4.7 48.4 1.0
C6 B:FAD501 4.7 47.6 1.0
C10 B:FAD501 4.7 43.0 1.0
NH2 B:ARG64 4.8 34.7 1.0
O B:GLY396 4.8 41.8 1.0
C9A B:FAD501 5.0 47.8 1.0

Chlorine binding site 2 out of 2 in 6esd

Go back to Chlorine Binding Sites List in 6esd
Chlorine binding site 2 out of 2 in the Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:71.2
occ:1.00
OH A:TYR309 3.0 46.4 1.0
NH1 A:ARG64 3.2 45.5 1.0
N5 A:FAD501 3.8 45.6 1.0
NE2 A:HIS163 3.8 54.9 1.0
C4X A:FAD501 4.0 42.7 1.0
CD2 A:HIS163 4.0 52.2 1.0
CZ A:TYR309 4.1 49.2 1.0
CE2 A:TYR309 4.2 48.9 1.0
CZ A:ARG64 4.2 43.4 1.0
C4 A:FAD501 4.3 43.0 1.0
C5X A:FAD501 4.3 47.6 1.0
NE A:ARG64 4.4 39.1 1.0
O4 A:FAD501 4.4 43.0 1.0
CH2 A:TRP397 4.5 43.9 1.0
CZ2 A:TRP397 4.6 42.7 1.0
C10 A:FAD501 4.7 45.1 1.0
C6 A:FAD501 4.8 48.8 1.0
CZ3 A:TRP397 4.9 43.4 1.0
O A:GLY396 4.9 42.0 1.0

Reference:

H.E.Lai, S.M.Chee, M.Morgan, S.Moore, K.Polizzi, P.Freemont. A Semi-Synthetic Strategy For Derivatization of the Violacein Natural Product Scaffold Biorxiv 2017.
DOI: 10.1101/202523
Page generated: Sat Jul 12 13:35:52 2025

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