7VDO
Crystal structure of KRED F147L/L153Q/Y190P variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide 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 | 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 | 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 | 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 PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SieglvgdptQgaYNASKGAVrIMSkSAA |
| Chain | Residue | Details |
| D | SER143-ALA171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:26644568 |
| Chain | Residue | Details |
| D | TYR156 | |
| A | TYR156 | |
| B | TYR156 | |
| C | TYR156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF2 |
| Chain | Residue | Details |
| D | TYR156 | |
| D | LYS160 | |
| D | ILE191 | |
| A | THR16 | |
| A | ARG39 | |
| A | ASP63 | |
| A | ASN90 | |
| A | TYR156 | |
| A | LYS160 | |
| A | ILE191 | |
| B | THR16 | |
| B | ARG39 | |
| B | ASP63 | |
| B | ASN90 | |
| B | TYR156 | |
| B | LYS160 | |
| B | ILE191 | |
| C | THR16 | |
| C | ARG39 | |
| C | ASP63 | |
| C | ASN90 | |
| C | TYR156 | |
| C | LYS160 | |
| C | ILE191 | |
| D | THR16 | |
| D | ARG39 | |
| D | ASP63 | |
| D | ASN90 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF4 |
| Chain | Residue | Details |
| D | GLN252 | |
| A | GLN252 | |
| B | GLN252 | |
| C | GLN252 |
