3GDF
Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019594 | biological_process | mannitol metabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019594 | biological_process | mannitol metabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019594 | biological_process | mannitol metabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019594 | biological_process | mannitol metabolic process |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1003 |
| Chain | Residue |
| A | GLU123 |
| A | HIS127 |
| D | GLU86 |
| D | GLU89 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1004 |
| Chain | Residue |
| A | ARG267 |
| A | HOH376 |
| A | HOH551 |
| D | ARG267 |
| D | HOH366 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1001 |
| Chain | Residue |
| B | ARG267 |
| C | ARG267 |
| C | HOH349 |
| C | HOH436 |
| C | HOH552 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1002 |
| Chain | Residue |
| B | GLU123 |
| B | HIS127 |
| C | GLU86 |
| C | GLU89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20420880 |
| Chain | Residue | Details |
| A | SER160 | |
| B | SER160 | |
| C | SER160 | |
| D | SER160 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20420880 |
| Chain | Residue | Details |
| A | TYR175 | |
| B | TYR175 | |
| C | TYR175 | |
| D | TYR175 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Lowers pKa of active site Tyr => ECO:0000305|PubMed:20420880 |
| Chain | Residue | Details |
| A | LYS179 | |
| B | LYS179 | |
| C | LYS179 | |
| D | LYS179 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | ASN108 | |
| C | TYR175 | |
| C | LYS179 | |
| C | ILE207 | |
| D | ASN108 | |
| D | TYR175 | |
| D | LYS179 | |
| D | ILE207 | |
| A | TYR175 | |
| A | LYS179 | |
| A | ILE207 | |
| B | ASN108 | |
| B | TYR175 | |
| B | LYS179 | |
| B | ILE207 | |
| C | ASN108 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4 |
| Chain | Residue | Details |
| A | LYS141 | |
| A | THR209 | |
| B | LYS141 | |
| B | THR209 | |
| C | LYS141 | |
| C | THR209 | |
| D | LYS141 | |
| D | THR209 |
