1N61
Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state
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 | 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 3001 |
| Chain | Residue |
| A | HIS5 |
| A | HOH3982 |
| A | HOH4027 |
| A | HOH4087 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 3907 |
| Chain | Residue |
| A | ARG138 |
| A | CYS139 |
| A | GLN101 |
| A | CYS102 |
| A | GLY103 |
| A | CYS105 |
| A | CYS137 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 3908 |
| Chain | Residue |
| A | GLY41 |
| A | CYS42 |
| A | SER45 |
| A | CYS47 |
| A | GLY48 |
| A | CYS50 |
| A | CYS62 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CUN B 3921 |
| Chain | Residue |
| B | GLN240 |
| B | GLY272 |
| B | ALA385 |
| B | TYR386 |
| B | ARG387 |
| B | CYS388 |
| B | SER389 |
| B | TYR568 |
| B | GLY569 |
| B | GLU763 |
| B | MCN3920 |
| B | HOH4307 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MCN B 3920 |
| Chain | Residue |
| A | GLN101 |
| A | CYS139 |
| B | GLY270 |
| B | PHE271 |
| B | ARG387 |
| B | GLN528 |
| B | GLY529 |
| B | GLN530 |
| B | HIS532 |
| B | THR535 |
| B | THR567 |
| B | TYR568 |
| B | GLY569 |
| B | SER570 |
| B | ARG571 |
| B | SER572 |
| B | THR573 |
| B | CYS686 |
| B | THR688 |
| B | ILE690 |
| B | ASN691 |
| B | ILE694 |
| B | ILE695 |
| B | GLN698 |
| B | LYS759 |
| B | GLY760 |
| B | VAL761 |
| B | GLY762 |
| B | GLU763 |
| B | CUN3921 |
| B | HOH4002 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES D 4907 |
| Chain | Residue |
| D | GLN101 |
| D | CYS102 |
| D | GLY103 |
| D | CYS105 |
| D | CYS137 |
| D | ARG138 |
| D | CYS139 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES D 4908 |
| Chain | Residue |
| D | GLY41 |
| D | CYS42 |
| D | SER45 |
| D | HIS46 |
| D | CYS47 |
| D | GLY48 |
| D | CYS50 |
| D | CYS62 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CUN E 4921 |
| Chain | Residue |
| E | GLN240 |
| E | GLY272 |
| E | ALA385 |
| E | TYR386 |
| E | ARG387 |
| E | CYS388 |
| E | SER389 |
| E | TYR568 |
| E | GLY569 |
| E | GLU763 |
| E | MCN4920 |
| E | HOH5292 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MCN E 4920 |
| Chain | Residue |
| E | TYR568 |
| E | GLY569 |
| E | SER570 |
| E | ARG571 |
| E | SER572 |
| E | THR573 |
| E | CYS686 |
| E | THR688 |
| E | ILE690 |
| E | ASN691 |
| E | ILE694 |
| E | ILE695 |
| E | GLN698 |
| E | LYS759 |
| E | GLY760 |
| E | VAL761 |
| E | GLY762 |
| E | GLU763 |
| E | CUN4921 |
| E | HOH5038 |
| D | GLN101 |
| D | CYS139 |
| E | GLY270 |
| E | PHE271 |
| E | ARG387 |
| E | GLN528 |
| E | GLY529 |
| E | GLN530 |
| E | HIS532 |
| E | THR535 |
| E | THR567 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD F 4931 |
| Chain | Residue |
| D | SER45 |
| D | HIS46 |
| F | ARG29 |
| F | PRO30 |
| F | ALA32 |
| F | GLY33 |
| F | GLY34 |
| F | HIS35 |
| F | SER36 |
| F | LEU37 |
| F | ILE101 |
| F | ALA102 |
| F | ILE106 |
| F | GLY110 |
| F | THR111 |
| F | GLY114 |
| F | ASN115 |
| F | ASN118 |
| F | ASN123 |
| F | ASP124 |
| F | ILE161 |
| F | LEU167 |
| F | LYS185 |
| F | GLY191 |
| F | ASP192 |
| F | TYR193 |
| F | HOH4940 |
| F | HOH4944 |
| F | HOH4985 |
| F | HOH5006 |
| F | HOH5059 |
| F | HOH5153 |
| site_id | BC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD C 3932 |
| Chain | Residue |
| A | SER45 |
| A | HIS46 |
| C | ARG29 |
| C | PRO30 |
| C | ALA32 |
| C | GLY33 |
| C | GLY34 |
| C | HIS35 |
| C | SER36 |
| C | LEU37 |
| C | ILE101 |
| C | ALA102 |
| C | GLY110 |
| C | THR111 |
| C | GLY114 |
| C | ASN115 |
| C | ALA117 |
| C | ASN118 |
| C | ASN123 |
| C | ASP124 |
| C | LEU166 |
| C | LEU167 |
| C | LYS185 |
| C | GLY191 |
| C | ASP192 |
| C | TYR193 |
| C | HOH3938 |
| C | HOH3949 |
| C | HOH4003 |
| C | HOH4029 |
| C | HOH4056 |
| C | HOH4073 |
| C | HOH4205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995 |
| Chain | Residue | Details |
| C | ALA32 | |
| D | CYS47 | |
| D | CYS50 | |
| D | CYS62 | |
| D | CYS102 | |
| D | CYS105 | |
| D | CYS137 | |
| D | CYS139 | |
| C | THR111 | |
| F | ALA32 | |
| F | THR111 | |
| A | CYS102 | |
| A | CYS105 | |
| A | CYS137 | |
| A | CYS139 | |
| D | CYS42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995 |
| Chain | Residue | Details |
| B | GLU763 | |
| E | GLU763 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | GLU763 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| E | GLU763 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | GLN240 | |
| B | ARG387 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| E | GLN240 | |
| E | ARG387 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 107 |
| Chain | Residue | Details |
| B | GLN240 | electrostatic stabiliser |
| B | ARG387 | electrostatic stabiliser |
| B | CYS388 | metal ligand |
| B | GLU763 | proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 107 |
| Chain | Residue | Details |
| E | GLN240 | electrostatic stabiliser |
| E | ARG387 | electrostatic stabiliser |
| E | CYS388 | metal ligand |
| E | GLU763 | proton acceptor, proton donor, proton relay |
