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

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 3B)

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 3B):
1.2.7.4; 2.3.1.169;

Other elements in 9fzz:

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 3B) also contains other interesting chemical elements:

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

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 3B) (pdb code 9fzz). 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 3B), PDB code: 9fzz:
Jump to Nickel binding site number: 1; 2; 3; 4;

Nickel binding site 1 out of 4 in 9fzz

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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 3B)


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 3B) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni802

b:88.0
occ:0.59
SG D:CYS488 2.1 94.0 1.0
SG D:CYS576 2.1 104.5 1.0
S1 D:SF4801 2.2 88.5 0.8
SG D:CYS574 2.2 97.8 1.0
FE4 D:SF4801 2.5 88.8 1.0
CB D:CYS488 3.2 94.5 1.0
NI D:NI803 3.3 97.5 0.8
CB D:CYS574 3.7 100.9 1.0
CB D:CYS576 3.8 107.8 1.0
CD1 D:LEU506 3.8 108.1 1.0
FE2 D:SF4801 3.9 87.5 0.9
FE3 D:SF4801 4.0 90.4 0.8
S3 D:SF4801 4.2 86.7 0.9
CB D:CYS507 4.2 104.2 1.0
NE2 D:HIS495 4.2 93.3 1.0
CD2 D:HIS495 4.4 94.1 1.0
S2 D:SF4801 4.4 88.3 0.7
CZ D:PHE491 4.6 110.6 1.0
CA D:CYS488 4.6 95.9 1.0
N D:CYS576 4.6 108.9 1.0
N D:CYS507 4.7 105.8 1.0
CG D:LEU506 4.8 107.2 1.0
CA D:CYS576 4.8 109.1 1.0
CA D:CYS507 4.8 105.7 1.0
SG D:CYS497 4.9 90.6 1.0
CA D:CYS574 5.0 102.9 1.0

Nickel binding site 2 out of 4 in 9fzz

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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 3B)


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 3B) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni803

b:97.5
occ:0.78
N D:CYS576 1.9 108.9 1.0
N D:GLY575 2.0 106.5 1.0
SG D:CYS574 2.2 97.8 1.0
SG D:CYS576 2.2 104.5 1.0
C D:GLY575 2.7 109.7 1.0
CA D:GLY575 2.8 108.3 1.0
CA D:CYS576 2.9 109.1 1.0
CB D:CYS574 3.0 100.9 1.0
C D:CYS574 3.0 105.4 1.0
CB D:CYS576 3.1 107.8 1.0
NI D:NI802 3.3 88.0 0.6
CA D:CYS574 3.3 102.9 1.0
N D:PHE577 3.6 112.1 1.0
N D:CYS574 3.7 103.0 1.0
C D:CYS576 3.7 111.1 1.0
CD1 D:LEU506 3.9 108.1 1.0
O D:GLY575 3.9 110.1 1.0
CZ D:PHE491 4.0 110.6 1.0
O D:CYS574 4.1 107.5 1.0
CD2 D:PHE577 4.1 109.5 1.0
CE2 D:PHE491 4.1 110.3 1.0
SG D:CYS488 4.4 94.0 1.0
CE2 D:PHE577 4.5 109.3 1.0
O D:CYS576 4.9 111.4 1.0
CA D:PHE577 4.9 113.6 1.0
CG D:PHE577 4.9 109.8 1.0
C D:SER573 4.9 103.9 1.0

Nickel binding site 3 out of 4 in 9fzz

Go back to Nickel Binding Sites List in 9fzz
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 3B)


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 3B) 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 41.9 1.0
S1 B:RQM703 2.3 26.5 0.9
S4 B:RQM703 2.4 26.6 0.8
FE2 B:RQM703 2.5 30.6 0.6
FE3 B:RQM703 3.0 25.2 1.0
FE1 B:RQM703 3.2 25.0 1.0
S3 B:RQM703 3.3 27.5 0.9
CB B:CYS523 3.4 37.5 1.0
FE4 B:RQM703 3.5 24.6 1.0
SG B:CYS295 4.0 35.5 1.0
NE2 B:HIS259 4.2 38.6 1.0
NZ B:LYS560 4.4 29.7 1.0
S2 B:RQM703 4.5 24.8 1.0
CA B:CYS523 4.7 32.9 1.0
CE B:LYS560 4.8 30.2 1.0
CD2 B:HIS259 4.9 35.1 1.0
SG B:CYS451 5.0 24.8 1.0

Nickel binding site 4 out of 4 in 9fzz

Go back to Nickel Binding Sites List in 9fzz
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 3B)


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 3B) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ni702

b:30.1
occ:0.51
NI C:RQM702 0.0 30.1 0.5
SG C:CYS523 2.1 41.6 1.0
S1 C:RQM702 2.3 26.6 1.0
S4 C:RQM702 2.4 26.5 0.8
FE2 C:RQM702 2.5 30.6 0.6
FE3 C:RQM702 3.0 25.2 1.0
FE1 C:RQM702 3.2 24.9 1.0
CB C:CYS523 3.3 37.0 1.0
S3 C:RQM702 3.3 27.4 0.9
FE4 C:RQM702 3.5 24.6 1.0
SG C:CYS295 4.0 35.6 1.0
NE2 C:HIS259 4.2 38.6 1.0
NZ C:LYS560 4.4 29.6 1.0
S2 C:RQM702 4.5 24.8 1.0
CA C:CYS523 4.7 32.5 1.0
CE C:LYS560 4.9 30.1 1.0
CD2 C:HIS259 5.0 35.1 1.0
SG C:CYS451 5.0 24.8 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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