3CV7
Crystal structure of porcine aldehyde reductase ternary complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
| A | 0042840 | biological_process | D-glucuronate catabolic process |
| A | 0046185 | biological_process | aldehyde catabolic process |
| A | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| A | 0047939 | molecular_function | L-glucuronate reductase activity |
| A | 0047941 | molecular_function | glucuronolactone reductase activity |
| A | 0047956 | molecular_function | glycerol dehydrogenase [NADP+] activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| A | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 361 |
| Chain | Residue |
| A | ARG251 |
| A | PHE277 |
| A | HOH539 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 362 |
| Chain | Residue |
| A | ARG167 |
| A | ARG243 |
| A | GLN275 |
| A | HOH505 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 363 |
| Chain | Residue |
| A | LYS13 |
| A | HOH398 |
| A | CYS5 |
| A | LEU7 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 364 |
| Chain | Residue |
| A | LEU303 |
| A | THR304 |
| A | HOH604 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP A 370 |
| Chain | Residue |
| A | GLY20 |
| A | THR21 |
| A | TRP22 |
| A | ASP45 |
| A | TYR50 |
| A | LYS80 |
| A | HIS113 |
| A | SER162 |
| A | ASN163 |
| A | GLN184 |
| A | TYR210 |
| A | SER211 |
| A | PRO212 |
| A | LEU213 |
| A | GLY214 |
| A | SER215 |
| A | ASP217 |
| A | ALA246 |
| A | ILE261 |
| A | PRO262 |
| A | LYS263 |
| A | SER264 |
| A | THR266 |
| A | ARG269 |
| A | GLN272 |
| A | ASN273 |
| A | HOH372 |
| A | HOH415 |
| A | HOH432 |
| A | HOH441 |
| A | HOH483 |
| A | HOH608 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE C2U A 371 |
| Chain | Residue |
| A | TRP22 |
| A | ILE49 |
| A | TYR50 |
| A | TRP82 |
| A | HIS113 |
| A | TRP114 |
| A | ARG312 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LealvakglVRALGLSNF |
| Chain | Residue | Details |
| A | LEU147-PHE164 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpsRIlQNiQV |
| Chain | Residue | Details |
| A | ILE261-VAL276 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAaiygnEleIG |
| Chain | Residue | Details |
| A | GLY40-GLY57 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:7552731 |
| Chain | Residue | Details |
| A | TYR50 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY11 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O60218 |
| Chain | Residue | Details |
| A | ASP45 | |
| A | SER162 | |
| A | GLN184 | |
| A | THR21 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7552731 |
| Chain | Residue | Details |
| A | SER211 | |
| A | HIS113 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550 |
| Chain | Residue | Details |
| A | LYS80 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P14550 |
| Chain | Residue | Details |
| A | ALA2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51635 |
| Chain | Residue | Details |
| A | SER4 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JII6 |
| Chain | Residue | Details |
| A | LYS127 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JII6 |
| Chain | Residue | Details |
| A | LYS145 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14550 |
| Chain | Residue | Details |
| A | SER211 |
