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Chlorine in PDB 3lx4: Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg)

Enzymatic activity of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg)

All present enzymatic activity of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg):
1.18.99.1;

Protein crystallography data

The structure of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg), PDB code: 3lx4 was solved by D.W.Mulder, E.S.Boyd, R.Sarma, R.K.Lange, J.A.Endrizzi, J.B.Broderick, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.97
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 70.895, 70.895, 155.429, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 21.6

Other elements in 3lx4:

The structure of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg) also contains other interesting chemical elements:

Iron (Fe) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg) (pdb code 3lx4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg), PDB code: 3lx4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3lx4

Go back to Chlorine Binding Sites List in 3lx4
Chlorine binding site 1 out of 2 in the Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl459

b:16.6
occ:1.00
O A:HOH731 3.1 31.6 1.0
NZ A:LYS188 3.3 21.0 1.0
N A:GLN155 3.3 11.0 1.0
CD A:PRO154 3.6 18.3 1.0
CG A:GLN155 3.7 14.3 1.0
CB A:SER153 3.7 15.6 1.0
CB A:GLN155 3.7 10.4 1.0
O A:ACT460 3.8 45.9 1.0
OG A:SER153 3.8 14.6 1.0
CB A:PRO154 3.9 12.4 1.0
N A:PRO154 3.9 11.2 1.0
CE A:LYS188 3.9 20.1 1.0
CG A:PRO154 4.0 11.9 1.0
CA A:GLN155 4.1 14.1 1.0
SG A:CYS129 4.1 16.6 0.2
C A:PRO154 4.2 14.6 1.0
CA A:PRO154 4.2 10.8 1.0
CD A:LYS188 4.4 14.9 1.0
SD A:MET183 4.4 18.7 1.0
C A:SER153 4.5 15.5 1.0
CE A:MET183 4.5 15.3 1.0
CD A:GLN155 4.6 10.7 1.0
CA A:SER153 4.6 13.2 1.0
OE2 A:GLU191 4.7 19.1 1.0
CG2 A:THR90 4.8 17.3 1.0
C A:ACT460 4.8 49.0 1.0

Chlorine binding site 2 out of 2 in 3lx4

Go back to Chlorine Binding Sites List in 3lx4
Chlorine binding site 2 out of 2 in the Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl459

b:16.3
occ:1.00
O B:HOH482 3.0 30.6 1.0
NZ B:LYS188 3.2 20.6 1.0
N B:GLN155 3.3 12.3 1.0
CG B:GLN155 3.6 14.5 1.0
CD B:PRO154 3.6 17.6 1.0
CB B:GLN155 3.7 11.8 1.0
CB B:SER153 3.7 15.9 1.0
OG B:SER153 3.8 13.2 1.0
CE B:LYS188 3.8 21.0 1.0
OXT B:ACT460 3.8 51.5 1.0
N B:PRO154 3.9 11.6 1.0
CB B:PRO154 3.9 11.8 1.0
CG B:PRO154 4.1 11.6 1.0
CA B:GLN155 4.1 13.9 1.0
SG B:CYS129 4.1 17.0 0.2
C B:PRO154 4.2 13.8 1.0
CA B:PRO154 4.3 10.6 1.0
SD B:MET183 4.4 19.0 1.0
CD B:LYS188 4.5 14.8 1.0
C B:SER153 4.5 15.4 1.0
CE B:MET183 4.5 14.9 1.0
CD B:GLN155 4.6 11.7 1.0
OE2 B:GLU191 4.6 18.5 1.0
CA B:SER153 4.7 13.0 1.0
CG2 B:THR90 4.7 17.2 1.0
C B:ACT460 4.8 51.9 1.0

Reference:

D.W.Mulder, E.S.Boyd, R.Sarma, R.K.Lange, J.A.Endrizzi, J.B.Broderick, J.W.Peters. Stepwise [Fefe]-Hydrogenase H-Cluster Assembly Revealed in the Structure of Hyda(Deltaefg). Nature V. 465 248 2010.
ISSN: ISSN 0028-0836
PubMed: 20418861
DOI: 10.1038/NATURE08993
Page generated: Sat Dec 12 09:53:56 2020

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