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Chlorine in PDB 4mab: Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation

Enzymatic activity of Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation

All present enzymatic activity of Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation:
1.11.1.15;

Protein crystallography data

The structure of Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation, PDB code: 4mab was solved by A.Perkins, K.J.Nelson, J.R.Williams, L.B.Poole, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.15 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 127.230, 172.420, 136.210, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23.9

Other elements in 4mab:

The structure of Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation also contains other interesting chemical elements:

Potassium (K) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation (pdb code 4mab). 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 Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation, PDB code: 4mab:

Chlorine binding site 1 out of 1 in 4mab

Go back to Chlorine Binding Sites List in 4mab
Chlorine binding site 1 out of 1 in the Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Resolving Cys to Ala Variant of Salmonella Alkyl Hydroperoxide Reductase C in Its Substrate-Ready Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl202

b:68.2
occ:1.00
H D:ILE3 2.3 38.8 1.0
HB2 D:SER1 2.5 93.6 1.0
O C:HOH1102 2.7 63.8 1.0
H D:LEU2 2.8 70.7 1.0
HG22 D:ILE3 3.1 44.3 1.0
N D:ILE3 3.1 37.3 1.0
HB D:ILE3 3.1 44.3 1.0
N D:LEU2 3.1 40.9 1.0
HD12 D:ILE133 3.2 47.7 1.0
HA D:SER1 3.2 78.3 1.0
HG11 C:VAL135 3.2 48.8 1.0
CB D:SER1 3.3 64.8 1.0
HG21 C:VAL135 3.3 41.3 1.0
CA D:SER1 3.5 62.6 1.0
C D:SER1 3.6 62.6 1.0
CB D:ILE3 3.7 39.6 1.0
CG2 D:ILE3 3.7 38.5 1.0
CD1 D:ILE133 3.9 36.8 1.0
C D:LEU2 3.9 37.1 1.0
CA D:LEU2 4.0 38.6 1.0
HB3 D:SER1 4.0 93.6 1.0
CA D:ILE3 4.0 37.1 1.0
HD11 D:ILE133 4.0 47.7 1.0
OG D:SER1 4.0 64.7 1.0
HG21 D:ILE3 4.0 44.3 1.0
HD13 D:ILE133 4.0 47.7 1.0
O C:HOH1090 4.0 61.1 1.0
CG1 C:VAL135 4.2 37.3 1.0
CG2 C:VAL135 4.2 37.7 1.0
HB2 D:LEU2 4.2 41.0 1.0
HG D:SER1 4.2 98.0 1.0
HB C:VAL135 4.3 39.3 1.0
CB C:VAL135 4.5 37.4 1.0
HA D:ILE3 4.5 33.9 1.0
O C:HOH1077 4.5 50.9 1.0
HG23 D:ILE3 4.6 44.3 1.0
O D:SER1 4.6 60.9 1.0
HG13 C:VAL135 4.7 48.8 1.0
CB D:LEU2 4.7 37.8 1.0
HG12 C:VAL135 4.7 48.8 1.0
HG22 C:VAL135 4.7 41.3 1.0
HG23 C:VAL135 4.8 41.3 1.0
HA D:LEU2 4.8 53.5 1.0
O C:ASP108 5.0 48.5 1.0

Reference:

A.Perkins, K.J.Nelson, J.R.Williams, D.Parsonage, L.B.Poole, P.A.Karplus. The Sensitive Balance Between the Fully Folded and Locally Unfolded Conformations of A Model Peroxiredoxin. Biochemistry V. 52 8708 2013.
ISSN: ISSN 0006-2960
PubMed: 24175952
DOI: 10.1021/BI4011573
Page generated: Sun Jul 21 19:38:58 2024

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