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Chlorine in PDB 9b01: Catalytic Mutant C357A Nnha in Ches Buffer

Enzymatic activity of Catalytic Mutant C357A Nnha in Ches Buffer

All present enzymatic activity of Catalytic Mutant C357A Nnha in Ches Buffer:
3.5.99.9;

Protein crystallography data

The structure of Catalytic Mutant C357A Nnha in Ches Buffer, PDB code: 9b01 was solved by T.S.Peat, J.Newman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.00 / 1.99
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 206.124, 206.124, 68.215, 90, 90, 120
R / Rfree (%) 14.6 / 17.4

Other elements in 9b01:

The structure of Catalytic Mutant C357A Nnha in Ches Buffer also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Mutant C357A Nnha in Ches Buffer (pdb code 9b01). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Catalytic Mutant C357A Nnha in Ches Buffer, PDB code: 9b01:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 9b01

Go back to Chlorine Binding Sites List in 9b01
Chlorine binding site 1 out of 2 in the Catalytic Mutant C357A Nnha in Ches Buffer


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Mutant C357A Nnha in Ches Buffer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:22.8
occ:1.00
OG A:SER29 3.1 15.0 1.0
CB A:SER29 3.8 15.2 1.0
CD2 A:TYR31 3.9 12.7 1.0
CB A:TYR31 4.0 12.7 1.0
CG A:GLU32 4.3 16.9 1.0
CG A:TYR31 4.4 12.2 1.0
CD A:GLU32 4.5 18.5 1.0
OE2 A:GLU32 4.6 19.1 1.0
N A:GLU32 4.7 12.4 1.0
OE1 A:GLU32 5.0 19.3 1.0
CE2 A:TYR31 5.0 13.2 1.0

Chlorine binding site 2 out of 2 in 9b01

Go back to Chlorine Binding Sites List in 9b01
Chlorine binding site 2 out of 2 in the Catalytic Mutant C357A Nnha in Ches Buffer


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Catalytic Mutant C357A Nnha in Ches Buffer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:54.8
occ:1.00
O A:HOH592 3.4 28.6 1.0
O A:HOH902 3.4 46.5 1.0
O A:GLU48 3.6 13.8 1.0
C A:GLU48 3.8 13.7 1.0
N A:PRO49 4.0 13.7 1.0
N A:ARG53 4.0 15.1 1.0
CB A:GLU48 4.1 13.6 1.0
CA A:PRO49 4.1 13.9 1.0
C A:ARG53 4.2 16.8 1.0
CA A:ARG53 4.3 15.3 1.0
O A:ARG53 4.3 13.9 1.0
C A:GLY52 4.4 13.6 1.0
O A:HOH524 4.5 31.0 1.0
CA A:GLU48 4.5 13.5 1.0
CG A:PRO49 4.6 12.8 1.0
CD A:PRO49 4.6 13.2 1.0
O A:HOH531 4.7 26.2 1.0
N A:THR54 4.7 16.4 1.0
O A:GLY52 4.9 12.8 1.0
CA A:GLY52 4.9 12.5 1.0
CB A:PRO49 4.9 13.7 1.0

Reference:

F.H.Ahmed, J.W.Liu, S.Royan, A.C.Warden, L.Esquirol, G.Pandey, J.Newman, C.Scott, T.S.Peat. Structural Insights Into the Enzymatic Breakdown of Azomycin-Derived Antibiotics By 2-Nitroimdazole Hydrolase (Nnha). Commun Biol V. 7 1676 2024.
ISSN: ESSN 2399-3642
PubMed: 39702827
DOI: 10.1038/S42003-024-07336-6
Page generated: Sun Jul 13 16:01:15 2025

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