4GQ0
Crystal structure of AKR1B10 complexed with NADP+ and Caffeic acid phenethyl ester
Replaces: 3V9QFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006060 | biological_process | sorbitol metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0006700 | biological_process | C21-steroid hormone biosynthetic process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0043795 | molecular_function | glyceraldehyde oxidoreductase activity |
| A | 0044597 | biological_process | daunorubicin metabolic process |
| A | 0044598 | biological_process | doxorubicin metabolic process |
| A | 0046370 | biological_process | fructose biosynthetic process |
| A | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| A | 0047939 | molecular_function | L-glucuronate reductase activity |
| A | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| A | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071475 | biological_process | cellular hyperosmotic salinity response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE QAP A 401 |
| Chain | Residue |
| A | TRP21 |
| A | TYR49 |
| A | HIS111 |
| A | PHE123 |
| A | PRO124 |
| A | LYS125 |
| A | LEU302 |
| A | NAP402 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP A 402 |
| Chain | Residue |
| A | THR20 |
| A | TRP21 |
| A | LYS22 |
| A | ASP44 |
| A | TYR49 |
| A | HIS111 |
| A | SER160 |
| A | ASN161 |
| A | GLN184 |
| A | TYR210 |
| A | SER211 |
| A | PRO212 |
| A | LEU213 |
| A | GLY214 |
| A | SER215 |
| A | PRO216 |
| A | ASP217 |
| A | ALA246 |
| A | ILE261 |
| A | PRO262 |
| A | LYS263 |
| A | SER264 |
| A | VAL265 |
| A | THR266 |
| A | ARG269 |
| A | GLU272 |
| A | ASN273 |
| A | QAP401 |
| A | HOH525 |
| A | HOH542 |
| A | HOH573 |
| A | HOH579 |
| A | HOH672 |
| A | GLY19 |
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 |
| A | 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 |
| A | ILE261-VAL276 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAyvyqnEheVG |
| Chain | Residue | Details |
| A | 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":"15272156","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18087047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of active site Tyr"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 62 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15146478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15272156","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16337231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17368668","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17418233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17505104","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"8281941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07943","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 725 |
| Chain | Residue | Details |
| A | ASP44 | electrostatic stabiliser |
| A | TYR49 | proton acceptor, proton donor |
| A | LYS78 | electrostatic stabiliser, modifies pKa |
| A | HIS111 | electrostatic stabiliser |
