3GDG
Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1002 |
| Chain | Residue |
| A | ARG267 |
| A | HOH304 |
| A | HOH419 |
| D | ARG267 |
| D | HOH269 |
| D | HOH668 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1001 |
| Chain | Residue |
| B | HOH317 |
| B | HOH327 |
| C | ARG267 |
| B | ARG267 |
| B | HOH296 |
| B | HOH298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"20420880","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"L0E2Z4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
