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Chlorine in PDB 7nem: Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form

Enzymatic activity of Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form

All present enzymatic activity of Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form:
1.12.99.6;

Protein crystallography data

The structure of Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form, PDB code: 7nem was solved by S.B.Carr, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.80 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 99.402, 100.252, 168.536, 90, 90, 90
R / Rfree (%) 15 / 16.7

Other elements in 7nem:

The structure of Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Nickel (Ni) 2 atoms
Iron (Fe) 24 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form (pdb code 7nem). 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 Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form, PDB code: 7nem:

Chlorine binding site 1 out of 1 in 7nem

Go back to Chlorine Binding Sites List in 7nem
Chlorine binding site 1 out of 1 in the Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hydrogenase-2 Variant R479K - Anaerobically Oxidised Form within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Cl605

b:19.3
occ:1.00
O T:HOH668 3.0 37.3 1.0
O M:HOH972 3.1 22.2 1.0
N M:LEU229 3.2 11.6 1.0
CA M:ASN228 3.6 10.9 1.0
O M:HOH878 3.8 29.2 1.0
CG M:LEU229 3.9 16.7 1.0
C M:ASN228 3.9 11.5 1.0
CG2 M:ILE450 4.0 14.8 1.0
NH2 T:ARG216 4.0 15.7 1.0
CB M:LEU229 4.1 14.5 1.0
CB M:HIS455 4.2 13.4 1.0
N M:ASN228 4.2 10.3 1.0
O M:ILE227 4.2 11.7 1.0
CG2 M:ILE227 4.3 12.6 1.0
OD1 M:ASN228 4.3 13.1 1.0
CA M:LEU229 4.3 12.6 1.0
C M:ILE227 4.5 11.0 1.0
CD1 M:LEU229 4.5 21.2 1.0
CB M:ASN228 4.7 11.0 1.0
CG M:ASN228 4.9 12.3 1.0
ND1 M:HIS455 4.9 18.9 1.0
CG M:HIS455 5.0 14.8 1.0
CD2 M:LEU229 5.0 20.7 1.0

Reference:

R.M.Evans, S.E.Beaton, L.Kertiss, W.K.Myers, S.B.Carr, F.A.Armstrong. A Comprehensive Structural and Kinetic Investigation of the Role of the Active-Site Argininein Bidirectional Hydrogen Activation By the [Nife]-Hydrogenase "Hyd-2) From Escherichia Coli To Be Published.
Page generated: Sun Jul 13 04:25:18 2025

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