Chlorine in PDB 6gl6: Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H

Enzymatic activity of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H

All present enzymatic activity of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H:
1.18.99.1;

Protein crystallography data

The structure of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H, PDB code: 6gl6 was solved by L.Kertess, T.Happe, E.Hofmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.730, 70.730, 155.900, 90.00, 90.00, 120.00
R / Rfree (%) 16.9 / 19.7

Other elements in 6gl6:

The structure of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H (pdb code 6gl6). 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 Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H, PDB code: 6gl6:

Chlorine binding site 1 out of 1 in 6gl6

Go back to Chlorine Binding Sites List in 6gl6
Chlorine binding site 1 out of 1 in the Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:25.9
occ:1.00
 HZ2 A:LYS188 2.4 30.5 1.0
H A:GLN155 2.5 27.4 1.0
HD2 A:PRO154 2.9 27.9 1.0
HG2 A:GLN155 3.0 28.9 1.0
HB2 A:SER153 3.0 30.8 1.0
HB2 A:PRO154 3.1 28.3 1.0
HB3 A:GLN155 3.1 30.2 1.0
O A:HOH962 3.1 38.0 1.0
NZ A:LYS188 3.1 25.4 1.0
HZ1 A:LYS188 3.2 30.5 1.0
HE3 A:LYS188 3.3 26.7 1.0
N A:GLN155 3.3 22.8 1.0
CD A:PRO154 3.7 23.2 1.0
CE A:LYS188 3.7 22.3 1.0
CB A:GLN155 3.7 25.1 1.0
HD2 A:LYS188 3.7 25.9 1.0
HE1 A:MET183 3.7 28.5 1.0
CG A:GLN155 3.8 24.1 1.0
HG A:SER153 3.8 31.1 1.0
CB A:PRO154 3.8 23.6 1.0
HZ3 A:LYS188 3.8 30.5 1.0
CB A:SER153 3.9 25.7 1.0
HG21 A:THR90 3.9 29.8 1.0
N A:PRO154 3.9 22.8 1.0
HG2 A:PRO154 3.9 29.9 1.0
OG A:SER153 4.0 25.9 1.0
CG A:PRO154 4.0 24.9 1.0
CA A:GLN155 4.1 21.5 1.0
C A:PRO154 4.2 24.9 1.0
CA A:PRO154 4.2 23.8 1.0
HE3 A:MET183 4.3 28.5 1.0
CD A:LYS188 4.3 21.6 1.0
CE A:MET183 4.3 23.8 1.0
HG3 A:GLN155 4.4 28.9 1.0
SD A:MET183 4.4 25.7 1.0
HB3 A:SER153 4.5 30.8 1.0
HD3 A:PRO154 4.5 27.9 1.0
C A:SER153 4.5 25.2 1.0
HE2 A:LYS188 4.5 26.7 1.0
CG2 A:THR90 4.5 24.8 1.0
HG23 A:THR90 4.6 29.8 1.0
HB2 A:GLN155 4.6 30.2 1.0
HA A:GLN155 4.6 25.8 1.0
HG22 A:THR90 4.6 29.8 1.0
HB3 A:PRO154 4.7 28.3 1.0
CD A:GLN155 4.7 24.9 1.0
HB2 A:CYS129 4.7 34.0 1.0
CA A:SER153 4.8 27.2 1.0
H A:MET156 4.8 27.6 1.0
OE2 A:GLU191 4.9 27.5 1.0
HD3 A:LYS188 4.9 25.9 1.0
O A:HOH972 4.9 49.6 1.0
HA A:SER153 4.9 32.7 1.0

Reference:

P.Rodriguez-Macia, L.Kertess, J.Burnik, J.A.Birrell, E.Hofmann, W.Lubitz, T.Happe, O.Rudiger. His-Ligation to the [4FE-4S] Subcluster Tunes the Catalytic Bias of [Fefe] Hydrogenase. J.Am.Chem.Soc. V. 141 472 2019.
ISSN: ESSN 1520-5126
PubMed: 30545220
DOI: 10.1021/JACS.8B11149
Page generated: Sat Dec 12 13:02:01 2020

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