1FFV
CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0005506 | molecular_function | iron ion binding |
B | 0005507 | molecular_function | copper ion binding |
B | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030151 | molecular_function | molybdenum ion binding |
B | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0071949 | molecular_function | FAD binding |
D | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
E | 0005506 | molecular_function | iron ion binding |
E | 0005507 | molecular_function | copper ion binding |
E | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0030151 | molecular_function | molybdenum ion binding |
E | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES A 1907 |
Chain | Residue |
A | GLN100 |
A | CYS101 |
A | GLY102 |
A | CYS104 |
A | CYS136 |
A | ARG137 |
A | CYS138 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES A 1908 |
Chain | Residue |
A | SER45 |
A | HIS46 |
A | CYS47 |
A | GLY48 |
A | CYS50 |
A | LYS60 |
A | CYS62 |
A | GLY41 |
A | CYS42 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES D 1909 |
Chain | Residue |
D | GLN100 |
D | CYS101 |
D | GLY102 |
D | CYS104 |
D | CYS136 |
D | ARG137 |
D | CYS138 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES D 1910 |
Chain | Residue |
D | GLY41 |
D | CYS42 |
D | SER45 |
D | HIS46 |
D | CYS47 |
D | GLY48 |
D | CYS50 |
D | LYS60 |
D | CYS62 |
site_id | AC5 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE PCD B 1920 |
Chain | Residue |
A | GLN100 |
A | CYS138 |
B | GLN237 |
B | GLY266 |
B | GLY267 |
B | PHE268 |
B | GLY269 |
B | ALA382 |
B | TYR383 |
B | ARO384 |
B | CSZ385 |
B | GLN522 |
B | GLY523 |
B | GLN524 |
B | HIS526 |
B | THR529 |
B | TYR562 |
B | GLY563 |
B | SER564 |
B | ARG565 |
B | SER566 |
B | THR567 |
B | CYS680 |
B | THR682 |
B | ILE684 |
B | ASN685 |
B | ILE688 |
B | ILE689 |
B | GLN692 |
B | LYS753 |
B | GLY754 |
B | VAL755 |
B | ALA756 |
B | GLU757 |
B | HOH2240 |
B | HOH2389 |
B | HOH2390 |
B | HOH2391 |
site_id | AC6 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE PCD E 1921 |
Chain | Residue |
E | LYS753 |
E | GLY754 |
E | VAL755 |
E | ALA756 |
E | GLU757 |
E | HOH2087 |
E | HOH2188 |
E | HOH2355 |
E | HOH2367 |
E | HOH2414 |
D | GLN100 |
D | CYS138 |
E | GLN237 |
E | GLY266 |
E | GLY267 |
E | PHE268 |
E | GLY269 |
E | ALA382 |
E | TYR383 |
E | ARO384 |
E | CSZ385 |
E | GLN522 |
E | GLY523 |
E | GLN524 |
E | HIS526 |
E | THR529 |
E | THR561 |
E | TYR562 |
E | GLY563 |
E | SER564 |
E | ARG565 |
E | SER566 |
E | THR567 |
E | CYS680 |
E | THR682 |
E | ILE684 |
E | ASN685 |
E | ILE689 |
E | GLN692 |
site_id | AC7 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD C 1922 |
Chain | Residue |
A | SER45 |
A | HIS46 |
C | LYS29 |
C | LEU30 |
C | ALA32 |
C | GLY33 |
C | GLY34 |
C | HIS35 |
C | SER36 |
C | LEU37 |
C | ILE101 |
C | ALA102 |
C | GLY110 |
C | THR111 |
C | GLY114 |
C | ASP115 |
C | ALA117 |
C | HIS118 |
C | ASN123 |
C | ASP124 |
C | LEU161 |
C | VAL166 |
C | MET167 |
C | LYS185 |
C | GLY191 |
C | ASP192 |
C | TRP193 |
C | HOH1981 |
C | HOH2007 |
C | HOH2024 |
C | HOH2046 |
site_id | AC8 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD F 1923 |
Chain | Residue |
D | SER45 |
F | LYS29 |
F | LEU30 |
F | ALA32 |
F | GLY33 |
F | GLY34 |
F | HIS35 |
F | SER36 |
F | LEU37 |
F | ILE54 |
F | ILE101 |
F | ALA102 |
F | GLY110 |
F | THR111 |
F | GLY114 |
F | ASP115 |
F | ALA117 |
F | ASN123 |
F | ASP124 |
F | LEU161 |
F | VAL166 |
F | MET167 |
F | LYS185 |
F | GLY191 |
F | ASP192 |
F | TRP193 |
F | HOH1961 |
F | HOH1967 |
F | HOH2013 |
F | HOH2017 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DAKLLAGGHSL |
Chain | Residue | Details |
C | ASP27-LEU37 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
B | CSZ385 | |
D | CYS47 | |
D | CYS50 | |
D | CYS62 | |
D | CYS101 | |
D | CYS104 | |
D | CYS136 | |
D | CYS138 | |
B | GLU757 | |
E | CSZ385 | |
E | GLU757 | |
A | CYS101 | |
A | CYS104 | |
A | CYS136 | |
A | CYS138 | |
D | CYS42 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: 4-hydroxyarginine => ECO:0000269|PubMed:10966817 |
Chain | Residue | Details |
B | ARO384 | |
E | ARO384 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
B | GLU757 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
E | GLU757 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
B | GLN237 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
E | GLN237 |