3BCJ
Crystal structure of Aldose Reductase complexed with 2S4R (Stereoisomer of Fidarestat, 2S4S) at 0.78 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0001758 | molecular_function | retinal dehydrogenase activity |
| A | 0002070 | biological_process | epithelial cell maturation |
| A | 0003091 | biological_process | renal water homeostasis |
| 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 | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate 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 | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
| A | 0035809 | biological_process | regulation of urine volume |
| A | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0043066 | biological_process | negative regulation of apoptotic 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 |
| A | 0072205 | biological_process | metanephric collecting duct development |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP A 318 |
| Chain | Residue |
| A | GLY18 |
| A | GLN183 |
| A | TYR209 |
| A | SER210 |
| A | PRO211 |
| A | LEU212 |
| A | GLY213 |
| A | SER214 |
| A | PRO215 |
| A | ASP216 |
| A | ALA245 |
| A | THR19 |
| A | ILE260 |
| A | PRO261 |
| A | LYS262 |
| A | SER263 |
| A | THR265 |
| A | ARG268 |
| A | GLU271 |
| A | ASN272 |
| A | HOH1128 |
| A | HOH1129 |
| A | TRP20 |
| A | HOH1155 |
| A | HOH1248 |
| A | HOH1451 |
| A | HOH1491 |
| A | HOH1531 |
| A | HOH1553 |
| A | LYS21 |
| A | ASP43 |
| A | TYR48 |
| A | HIS110 |
| A | SER159 |
| A | ASN160 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT A 319 |
| Chain | Residue |
| A | TRP20 |
| A | TYR48 |
| A | TRP79 |
| A | HIS110 |
| A | TRP111 |
| A | CYS298 |
| A | HOH1302 |
| A | HOH1361 |
| A | HOH1445 |
| A | HOH1449 |
| A | HOH1450 |
| A | HOH1451 |
| A | HOH1663 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FIS A 320 |
| Chain | Residue |
| A | TRP20 |
| A | LYS21 |
| A | PRO218 |
| A | HOH1220 |
| A | HOH1266 |
| A | HOH1267 |
| A | HOH1297 |
| A | HOH1304 |
| A | HOH1386 |
| A | HOH1450 |
| A | HOH1547 |
| A | HOH1548 |
| A | HOH1549 |
| A | HOH1590 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGISNF |
| Chain | Residue | Details |
| A | MET144-PHE161 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfKV |
| Chain | Residue | Details |
| A | ILE260-VAL275 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAhvyqnEneVG |
| Chain | Residue | Details |
| A | GLY38-GLY55 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:15272156 |
| Chain | Residue | Details |
| A | TYR48 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS110 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15146478, ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231, ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233, ECO:0000269|PubMed:17505104 |
| Chain | Residue | Details |
| A | SER210 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Lowers pKa of active site Tyr |
| Chain | Residue | Details |
| A | LYS77 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:8281941, ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | ALA1 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07943 |
| Chain | Residue | Details |
| A | SER2 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS94 | |
| A | LYS221 | |
| A | LYS262 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 725 |
| Chain | Residue | Details |
| A | ASP43 | electrostatic stabiliser |
| A | TYR48 | proton acceptor, proton donor |
| A | LYS77 | electrostatic stabiliser, modifies pKa |
| A | HIS110 | electrostatic stabiliser |
