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 |