1CWN
CRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME
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 | 0160163 | molecular_function | S-nitrosoglutathione reductase (NADPH) activity |
| A | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NAP A 350 |
| Chain | Residue |
| A | GLY20 |
| A | TRP22 |
| A | SER211 |
| A | LEU213 |
| A | SER215 |
| A | PRO262 |
| A | SER264 |
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. IPKSVTpsRIpQNiQV |
| 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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11306083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7552731","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O60218","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11306083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11306083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CV7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P51635","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9JII6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JII6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS80 | |
| A | HIS113 | |
| A | ASP45 | |
| A | TYR50 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS80 | |
| A | TYR50 |
