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Nickel in PDB 9g00: Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)

Enzymatic activity of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)

All present enzymatic activity of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB):
1.2.7.4; 2.3.1.169;

Other elements in 9g00:

The structure of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) also contains other interesting chemical elements:

Cobalt (Co) 1 atom
Iron (Fe) 28 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) (pdb code 9g00). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 4 binding sites of Nickel where determined in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB), PDB code: 9g00:
Jump to Nickel binding site number: 1; 2; 3; 4;

Nickel binding site 1 out of 4 in 9g00

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Nickel binding site 1 out of 4 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni802

b:97.9
occ:0.45
SG D:CYS576 2.0 114.3 1.0
SG D:CYS574 2.1 114.2 1.0
SG D:CYS488 2.1 106.9 1.0
S1 D:SF4801 2.4 102.9 0.9
FE4 D:SF4801 2.4 103.0 0.8
NI D:NI803 3.1 100.2 0.7
CB D:CYS488 3.2 109.7 1.0
CB D:CYS574 3.4 114.7 1.0
CB D:CYS576 3.7 116.0 1.0
FE2 D:SF4801 4.0 103.9 0.8
S3 D:SF4801 4.1 103.6 0.7
FE3 D:SF4801 4.2 105.4 0.9
NE2 D:HIS495 4.2 110.6 1.0
S2 D:SF4801 4.3 104.1 0.9
CD2 D:HIS495 4.4 110.3 1.0
N D:CYS576 4.5 117.8 1.0
CA D:CYS488 4.6 111.4 1.0
CA D:CYS576 4.7 117.2 1.0
CA D:CYS574 4.8 114.8 1.0
CB D:CYS507 4.8 115.5 1.0
N D:CYS507 4.9 116.4 1.0
N D:GLY575 4.9 116.3 1.0
SG D:CYS497 4.9 109.0 1.0
CB D:LEU506 4.9 117.5 1.0

Nickel binding site 2 out of 4 in 9g00

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Nickel binding site 2 out of 4 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni803

b:100.2
occ:0.71
N D:CYS576 1.9 117.8 1.0
N D:GLY575 2.0 116.3 1.0
SG D:CYS574 2.2 114.2 1.0
SG D:CYS576 2.2 114.3 1.0
C D:GLY575 2.7 118.0 1.0
CA D:GLY575 2.8 117.2 1.0
CB D:CYS574 2.8 114.7 1.0
CA D:CYS576 2.9 117.2 1.0
C D:CYS574 2.9 115.1 1.0
CB D:CYS576 3.0 116.0 1.0
NI D:NI802 3.1 97.9 0.5
CA D:CYS574 3.2 114.8 1.0
N D:CYS574 3.6 115.4 1.0
N D:PHE577 3.6 123.1 1.0
C D:CYS576 3.7 119.5 1.0
O D:GLY575 3.9 119.7 1.0
O D:CYS574 4.1 116.2 1.0
CD2 D:PHE577 4.1 124.4 1.0
CZ D:PHE491 4.3 132.2 1.0
C46 F:B12502 4.5 180.1 1.0
CE2 D:PHE577 4.5 124.0 1.0
SG D:CYS488 4.6 106.9 1.0
CE2 D:PHE491 4.8 132.1 1.0
O D:CYS576 4.9 119.9 1.0
C D:SER573 4.9 118.0 1.0
CA D:PHE577 4.9 125.7 1.0
CG D:PHE577 4.9 125.2 1.0
S1 D:SF4801 5.0 102.9 0.9

Nickel binding site 3 out of 4 in 9g00

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Nickel binding site 3 out of 4 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ni703

b:29.9
occ:0.50
NI B:RQM703 0.0 29.9 0.5
SG B:CYS523 2.1 42.1 1.0
S1 B:RQM703 2.3 26.6 0.9
S4 B:RQM703 2.4 26.7 0.8
FE2 B:RQM703 2.5 30.7 0.6
FE3 B:RQM703 3.0 25.3 0.9
FE1 B:RQM703 3.2 25.1 1.0
S3 B:RQM703 3.3 27.6 0.9
CB B:CYS523 3.4 37.6 1.0
FE4 B:RQM703 3.5 24.7 1.0
SG B:CYS295 4.0 35.8 1.0
NE2 B:HIS259 4.2 38.8 1.0
NZ B:LYS560 4.4 29.9 1.0
S2 B:RQM703 4.5 24.9 1.0
CA B:CYS523 4.7 33.0 1.0
CE B:LYS560 4.8 30.5 1.0
CD2 B:HIS259 4.9 35.3 1.0
SG B:CYS451 5.0 25.0 1.0

Nickel binding site 4 out of 4 in 9g00

Go back to Nickel Binding Sites List in 9g00
Nickel binding site 4 out of 4 in the Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 4 of Structure of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) in Complex with Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3CB) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ni702

b:30.2
occ:0.51
NI C:RQM702 0.0 30.2 0.5
SG C:CYS523 2.1 41.9 1.0
S1 C:RQM702 2.3 26.7 0.9
S4 C:RQM702 2.4 26.6 0.8
FE2 C:RQM702 2.5 30.6 0.6
FE3 C:RQM702 3.0 25.4 0.9
FE1 C:RQM702 3.2 25.0 1.0
CB C:CYS523 3.3 37.1 1.0
S3 C:RQM702 3.3 27.5 0.9
FE4 C:RQM702 3.5 24.7 1.0
SG C:CYS295 4.0 36.0 1.0
NE2 C:HIS259 4.2 38.8 1.0
NZ C:LYS560 4.4 29.8 1.0
S2 C:RQM702 4.5 24.9 1.0
CA C:CYS523 4.7 32.7 1.0
CE C:LYS560 4.9 30.4 1.0
CD2 C:HIS259 5.0 35.3 1.0
SG C:CYS451 5.0 25.0 1.0

Reference:

M.D.Yin, O.N.Lemaire, M.Belhamri, J.G.Rosas-Jimenez, G.Hummer, T.Wagner, B.J.Murphy. Snapshots of Acetyl-Coa Synthesis, the Last Step of CO2 Fixation in the Wood-Ljungdahl Pathway Science 2025.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADR9672
Page generated: Sun Feb 9 08:46:02 2025

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