3V35
Aldose reductase complexed with a nitro compound
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 | 0005739 | cellular_component | mitochondrion |
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 | 33 |
Details | BINDING SITE FOR RESIDUE NAP A 316 |
Chain | Residue |
A | GLY18 |
A | ASN160 |
A | GLN183 |
A | TYR209 |
A | SER210 |
A | PRO211 |
A | LEU212 |
A | GLY213 |
A | SER214 |
A | PRO215 |
A | ASP216 |
A | THR19 |
A | ALA245 |
A | ILE260 |
A | PRO261 |
A | LYS262 |
A | SER263 |
A | VAL264 |
A | THR265 |
A | ARG268 |
A | GLU271 |
A | ASN272 |
A | TRP20 |
A | DMF318 |
A | HOH402 |
A | HOH423 |
A | HOH466 |
A | LYS21 |
A | ASP43 |
A | TYR48 |
A | LYS77 |
A | HIS110 |
A | SER159 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NTI A 317 |
Chain | Residue |
A | TRP20 |
A | VAL47 |
A | TRP79 |
A | HIS110 |
A | TRP111 |
A | PRO218 |
A | TRP219 |
A | DMF318 |
A | DMF322 |
A | DMF329 |
A | DMF331 |
A | DMF332 |
A | DMF337 |
A | HOH430 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMF A 318 |
Chain | Residue |
A | TRP20 |
A | TYR48 |
A | HIS110 |
A | TRP111 |
A | NAP316 |
A | NTI317 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMF A 319 |
Chain | Residue |
A | LYS89 |
A | GLU150 |
A | TYR189 |
A | PRO225 |
A | ARG293 |
A | TRP295 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMF A 320 |
Chain | Residue |
A | TYR189 |
A | GLY213 |
A | ARG217 |
A | PRO225 |
A | SER226 |
A | LEU227 |
A | TRP295 |
A | HOH424 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMF A 321 |
Chain | Residue |
A | HIS46 |
A | THR81 |
A | TYR82 |
A | GLY118 |
A | LYS119 |
A | GLU120 |
A | PHE121 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE DMF A 322 |
Chain | Residue |
A | TRP20 |
A | VAL47 |
A | TYR48 |
A | GLN49 |
A | NTI317 |
A | DMF332 |
A | DMF340 |
A | HOH430 |
A | HOH570 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMF A 323 |
Chain | Residue |
A | GLY151 |
A | LYS154 |
A | ARG232 |
A | HOH607 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMF A 324 |
Chain | Residue |
A | ILE196 |
A | GLN200 |
A | ARG255 |
A | HOH394 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMF A 325 |
Chain | Residue |
A | GLN197 |
A | TYR198 |
A | HOH509 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMF A 326 |
Chain | Residue |
A | ASP139 |
A | PRO173 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMF A 327 |
Chain | Residue |
A | ASN8 |
A | GLY9 |
A | LYS154 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMF A 328 |
Chain | Residue |
A | ASN7 |
A | ASN8 |
A | ALA155 |
A | ILE156 |
A | LYS178 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMF A 329 |
Chain | Residue |
A | PHE122 |
A | LEU124 |
A | SER302 |
A | NTI317 |
A | DMF331 |
A | DMF337 |
A | HOH486 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMF A 330 |
Chain | Residue |
A | VAL148 |
A | ASP149 |
A | TYR177 |
A | SER290 |
A | HOH493 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMF A 331 |
Chain | Residue |
A | NTI317 |
A | DMF329 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMF A 332 |
Chain | Residue |
A | VAL47 |
A | PHE121 |
A | PHE122 |
A | NTI317 |
A | DMF322 |
A | HOH596 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMF A 333 |
Chain | Residue |
A | DMF336 |
A | HOH446 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMF A 334 |
Chain | Residue |
A | LEU175 |
A | LYS176 |
A | LYS178 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMF A 335 |
Chain | Residue |
A | GLN59 |
A | GLU60 |
A | ARG63 |
A | HOH598 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMF A 336 |
Chain | Residue |
A | LYS100 |
A | LEU101 |
A | ASP102 |
A | DMF333 |
A | HOH412 |
A | HOH446 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMF A 337 |
Chain | Residue |
A | TRP219 |
A | CYS298 |
A | ALA299 |
A | LEU300 |
A | NTI317 |
A | DMF329 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMF A 338 |
Chain | Residue |
A | ALA299 |
A | TYR309 |
A | PHE311 |
site_id | CC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMF A 339 |
Chain | Residue |
A | TRP295 |
A | ARG296 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMF A 340 |
Chain | Residue |
A | LYS21 |
A | PRO23 |
A | PRO24 |
A | TYR48 |
A | DMF322 |
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 |