4GAC
High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form
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 | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019640 | biological_process | D-glucuronate catabolic process to D-xylulose 5-phosphate |
| A | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
| A | 0042840 | biological_process | D-glucuronate catabolic process |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0044597 | biological_process | daunorubicin metabolic process |
| A | 0044598 | biological_process | doxorubicin metabolic process |
| A | 0045202 | cellular_component | synapse |
| 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 | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) 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 |
| B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| B | 0016324 | cellular_component | apical plasma membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019640 | biological_process | D-glucuronate catabolic process to D-xylulose 5-phosphate |
| B | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
| B | 0042840 | biological_process | D-glucuronate catabolic process |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0044597 | biological_process | daunorubicin metabolic process |
| B | 0044598 | biological_process | doxorubicin metabolic process |
| B | 0045202 | cellular_component | synapse |
| B | 0046185 | biological_process | aldehyde catabolic process |
| B | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| B | 0047939 | molecular_function | L-glucuronate reductase activity |
| B | 0047941 | molecular_function | glucuronolactone reductase activity |
| B | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| B | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0160163 | molecular_function | S-nitrosoglutathione reductase (NADPH) activity |
| B | 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 EDO A 401 |
| Chain | Residue |
| A | TRP22 |
| A | TYR50 |
| A | HIS113 |
| A | ASN163 |
| A | TYR210 |
| A | HOH561 |
| A | HOH653 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FLC A 402 |
| Chain | Residue |
| A | SER264 |
| A | ARG269 |
| A | HOH557 |
| A | HOH563 |
| A | HOH584 |
| A | HOH603 |
| A | HOH626 |
| A | HOH695 |
| A | HOH1049 |
| B | ARG269 |
| B | HOH594 |
| A | ASP217 |
| A | LYS263 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 401 |
| Chain | Residue |
| B | HIS199 |
| B | ALA202 |
| B | ARG203 |
| B | HOH621 |
| B | HOH835 |
| B | HOH888 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC B 402 |
| Chain | Residue |
| A | ARG269 |
| A | HOH593 |
| B | LEU213 |
| B | LEU229 |
| B | SER264 |
| B | ARG269 |
| B | HOH633 |
| B | HOH664 |
| B | HOH682 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LevlvakglVKALGLSNF |
| 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. IPKSINpsRIlQNiQV |
| Chain | Residue | Details |
| A | ILE261-VAL276 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAsvygnEteIG |
| Chain | Residue | Details |
| A | GLY40-GLY57 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O60218","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P50578","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P51635","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
