3S1L
Crystal Structure of Apo-form FurX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS42 |
| A | HIS65 |
| A | GLU66 |
| A | CYS152 |
| A | ARG335 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE P6G A 600 |
| Chain | Residue |
| A | THR44 |
| A | TRP53 |
| A | TRP91 |
| A | ASN115 |
| A | LEU266 |
| A | ILE289 |
| A | VAL290 |
| A | HOH423 |
| A | HOH468 |
| A | HOH750 |
| A | HOH753 |
| A | HOH797 |
| A | HOH905 |
| B | LEU280 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | CYS96 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | CYS42 |
| B | HIS65 |
| B | GLU66 |
| B | CYS152 |
| B | ARG335 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE P6G B 600 |
| Chain | Residue |
| B | THR44 |
| B | TRP53 |
| B | TRP91 |
| B | ASN115 |
| B | ILE289 |
| B | VAL290 |
| B | HOH506 |
| B | HOH766 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 500 |
| Chain | Residue |
| C | CYS96 |
| C | CYS99 |
| C | CYS102 |
| C | CYS110 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | CYS42 |
| C | HIS65 |
| C | GLU66 |
| C | CYS152 |
| C | ARG335 |
| C | P6G600 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE P6G C 600 |
| Chain | Residue |
| C | THR44 |
| C | TRP53 |
| C | VAL55 |
| C | HIS65 |
| C | TRP91 |
| C | TYR118 |
| C | CYS152 |
| C | LEU266 |
| C | ILE289 |
| C | VAL290 |
| C | ZN501 |
| C | HOH628 |
| C | HOH755 |
| D | ARG257 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 500 |
| Chain | Residue |
| D | CYS96 |
| D | CYS99 |
| D | CYS102 |
| D | CYS110 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | CYS42 |
| D | HIS65 |
| D | GLU66 |
| D | CYS152 |
| D | ARG335 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE P6G D 600 |
| Chain | Residue |
| D | THR44 |
| D | TRP53 |
| D | TRP91 |
| D | CYS152 |
| D | LEU266 |
| D | ILE289 |
| D | HOH354 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGYvsavGsgV |
| Chain | Residue | Details |
| A | GLY64-VAL78 |
