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Chlorine in PDB 6gal: Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10

Enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10

All present enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10:
1.12.99.6;

Protein crystallography data

The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10, PDB code: 6gal was solved by S.B.Carr, F.A.Armstrong, R.M.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 92.12 / 1.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 94.906, 95.224, 183.910, 90.00, 90.00, 90.00
R / Rfree (%) 12 / 14.7

Other elements in 6gal:

The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10 also contains other interesting chemical elements:

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

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10 (pdb code 6gal). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10, PDB code: 6gal:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6gal

Go back to Chlorine Binding Sites List in 6gal
Chlorine binding site 1 out of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10 within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Cl404

b:13.5
occ:1.00
H S:GLY256 2.1 8.7 1.0
H S:CYS120 2.3 7.1 1.0
O S:HOH621 3.0 11.3 1.0
O S:HOH643 3.1 22.2 1.0
N S:GLY256 3.1 8.5 1.0
HB2 S:TRP118 3.2 10.8 1.0
HB3 S:TRP118 3.2 10.7 1.0
N S:CYS120 3.2 7.4 1.0
HA S:CYS120 3.2 7.3 1.0
HA2 S:GLY256 3.4 10.3 1.0
HG21 S:THR114 3.4 7.8 1.0
HA S:ASN255 3.5 8.7 1.0
HG23 S:THR114 3.5 7.7 1.0
CB S:TRP118 3.6 10.5 1.0
HG22 S:THR114 3.7 7.7 1.0
CA S:CYS120 3.7 7.1 1.0
CG2 S:THR114 3.7 7.8 1.0
CA S:GLY256 3.7 10.2 1.0
H S:PHE257 3.7 9.0 1.0
HD1 S:TRP258 3.8 7.2 1.0
C S:TRP118 4.0 8.5 1.0
N S:GLY119 4.1 7.3 1.0
HA3 S:GLY119 4.1 7.8 1.0
C S:ASN255 4.1 8.8 1.0
OD1 S:ASN255 4.1 12.4 1.0
C S:GLY119 4.2 6.9 1.0
HD1 S:PHE257 4.2 8.6 1.0
O S:TRP118 4.2 11.1 1.0
CA S:ASN255 4.2 8.7 1.0
CA S:GLY119 4.3 7.9 1.0
H S:GLY119 4.4 7.2 1.0
O S:CYS120 4.4 6.5 1.0
N S:PHE257 4.4 8.7 1.0
O S:GLU254 4.5 9.1 1.0
CA S:TRP118 4.5 8.9 1.0
O S:HOH650 4.5 19.9 1.0
C S:GLY256 4.5 9.1 1.0
C S:CYS120 4.5 7.0 1.0
HA3 S:GLY256 4.5 9.8 1.0
HB3 S:ALA123 4.6 8.1 1.0
CD1 S:TRP258 4.6 7.5 1.0
H S:TRP258 4.7 7.3 1.0
CG S:TRP118 4.7 14.2 1.0
O S:HOH632 4.8 27.9 1.0
HB2 S:CYS120 4.9 7.3 1.0
HE1 S:PHE257 4.9 8.6 1.0
CD1 S:PHE257 4.9 8.7 1.0
O S:THR114 4.9 7.7 1.0
HE1 S:TRP258 4.9 6.7 1.0
HD1 S:TRP118 4.9 14.8 1.0
CB S:CYS120 4.9 6.9 1.0

Chlorine binding site 2 out of 2 in 6gal

Go back to Chlorine Binding Sites List in 6gal
Chlorine binding site 2 out of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q Collected at pH 10 within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Cl404

b:13.5
occ:1.00
H T:GLY256 2.1 8.8 1.0
H T:CYS120 2.3 6.9 1.0
O T:HOH631 3.0 11.7 1.0
N T:GLY256 3.1 8.6 1.0
O T:HOH678 3.1 20.9 1.0
HB2 T:TRP118 3.2 10.5 1.0
HA T:CYS120 3.2 6.4 1.0
N T:CYS120 3.2 6.7 1.0
HB3 T:TRP118 3.2 10.2 1.0
HG21 T:THR114 3.4 7.7 1.0
HA2 T:GLY256 3.4 9.5 1.0
HA T:ASN255 3.5 9.1 1.0
HG23 T:THR114 3.6 7.8 1.0
CB T:TRP118 3.6 10.1 1.0
CA T:CYS120 3.7 6.6 1.0
HG22 T:THR114 3.8 7.7 1.0
CA T:GLY256 3.8 9.1 1.0
CG2 T:THR114 3.8 7.9 1.0
HD1 T:TRP258 3.8 7.1 1.0
H T:PHE257 3.8 7.9 1.0
HA3 T:GLY119 4.0 7.3 1.0
N T:GLY119 4.1 7.5 1.0
C T:TRP118 4.1 7.9 1.0
C T:ASN255 4.1 9.2 1.0
HD1 T:PHE257 4.2 8.8 1.0
OD1 T:ASN255 4.2 12.7 1.0
C T:GLY119 4.2 6.7 1.0
CA T:ASN255 4.2 9.0 1.0
O T:TRP118 4.3 10.4 1.0
CA T:GLY119 4.3 7.0 1.0
H T:GLY119 4.3 7.8 1.0
O T:CYS120 4.4 6.7 1.0
N T:PHE257 4.4 8.4 1.0
O T:GLU254 4.5 9.0 1.0
HB3 T:ALA123 4.5 7.8 1.0
C T:CYS120 4.5 6.2 1.0
C T:GLY256 4.5 8.7 1.0
CA T:TRP118 4.6 8.3 1.0
HA3 T:GLY256 4.6 9.1 1.0
O T:HOH684 4.6 19.4 1.0
CD1 T:TRP258 4.6 7.2 1.0
H T:TRP258 4.6 7.3 1.0
CG T:TRP118 4.7 12.9 1.0
O T:HOH672 4.8 28.4 1.0
HB2 T:CYS120 4.8 6.2 1.0
HE1 T:PHE257 4.8 8.8 1.0
CD1 T:PHE257 4.8 9.2 1.0
CB T:CYS120 4.9 6.4 1.0
HD1 T:TRP118 4.9 14.9 1.0
HE1 T:TRP258 4.9 6.7 1.0
O T:THR114 4.9 6.6 1.0

Reference:

R.M.Evans, P.A.Ash, S.E.Beaton, E.J.Brooke, K.A.Vincent, S.B.Carr, F.A.Armstrong. Mechanistic Exploitation of A Self-Repairing, Blocked Proton Transfer Pathway in An O2-Tolerant [Nife]-Hydrogenase. J. Am. Chem. Soc. V. 140 10208 2018.
ISSN: ESSN 1520-5126
PubMed: 30070475
DOI: 10.1021/JACS.8B04798
Page generated: Sat Jul 27 23:54:31 2024

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