Atomistry » Chlorine » PDB 6g8l-6ggl » 6gal
Atomistry »
  Chlorine »
    PDB 6g8l-6ggl »
      6gal »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy