4XZN
Crystal structure of the methylated K125R/V301L AKR1B10 Holoenzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0001523 | biological_process | retinoid metabolic process |
| X | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| X | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| X | 0005515 | molecular_function | protein binding |
| X | 0005576 | cellular_component | extracellular region |
| X | 0005739 | cellular_component | mitochondrion |
| X | 0005764 | cellular_component | lysosome |
| X | 0005829 | cellular_component | cytosol |
| X | 0006629 | biological_process | lipid metabolic process |
| X | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| X | 0016488 | biological_process | farnesol catabolic process |
| X | 0016491 | molecular_function | oxidoreductase activity |
| X | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| X | 0042572 | biological_process | retinol metabolic process |
| X | 0044597 | biological_process | daunorubicin metabolic process |
| X | 0044598 | biological_process | doxorubicin metabolic process |
| X | 0045550 | molecular_function | geranylgeranyl reductase activity |
| X | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| X | 0047718 | molecular_function | indanol dehydrogenase activity |
| X | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| X | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue NAP X 401 |
| Chain | Residue |
| X | GLY19 |
| X | TYR210 |
| X | SER211 |
| X | PRO212 |
| X | LEU213 |
| X | GLY214 |
| X | SER215 |
| X | PRO216 |
| X | ASP217 |
| X | ALA246 |
| X | ILE261 |
| X | THR20 |
| X | PRO262 |
| X | MLY263 |
| X | SER264 |
| X | VAL265 |
| X | THR266 |
| X | ARG269 |
| X | GLU272 |
| X | ASN273 |
| X | HOH502 |
| X | HOH512 |
| X | TRP21 |
| X | HOH520 |
| X | HOH524 |
| X | HOH590 |
| X | HOH615 |
| X | HOH618 |
| X | ASP44 |
| X | TYR49 |
| X | HIS111 |
| X | SER160 |
| X | ASN161 |
| X | GLN184 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO X 402 |
| Chain | Residue |
| X | GLU6 |
| X | HIS201 |
| X | GLY204 |
| X | THR206 |
| X | ASN257 |
| X | HOH672 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKALGVSNF |
| Chain | Residue | Details |
| X | MET145-PHE162 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpaRIvENiQV |
| Chain | Residue | Details |
| X | ILE261-VAL276 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAyvyqnEheVG |
| Chain | Residue | Details |
| X | GLY39-GLY56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18087047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18087047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
