3LN3
Crystal structure of Putative reductase (NP_038806.2) from MUS MUSCULUS at 1.18 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| A | 0031406 | molecular_function | carboxylic acid binding |
| A | 0032052 | molecular_function | bile acid binding |
| A | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| A | 0036131 | molecular_function | prostaglandin D2 11-ketoreductase activity |
| A | 0042448 | biological_process | progesterone metabolic process |
| A | 0044597 | biological_process | daunorubicin metabolic process |
| A | 0044598 | biological_process | doxorubicin metabolic process |
| A | 0045550 | molecular_function | geranylgeranyl reductase activity |
| A | 0045703 | molecular_function | ketoreductase activity |
| A | 0047020 | molecular_function | 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity |
| A | 0047023 | molecular_function | androsterone dehydrogenase [NAD(P)+] activity |
| A | 0047045 | molecular_function | testosterone dehydrogenase (NADP+) activity |
| A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
| A | 0047115 | molecular_function | trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity |
| A | 0047743 | molecular_function | chlordecone reductase activity |
| A | 0047787 | molecular_function | Delta4-3-oxosteroid 5beta-reductase activity |
| A | 0140169 | molecular_function | 3-alpha-hydroxysteroid 3-dehydrogenase [NAD(P)+] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 324 |
| Chain | Residue |
| A | ARG171 |
| A | ARG175 |
| A | HOH360 |
| A | HOH453 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 325 |
| Chain | Residue |
| A | HOH668 |
| A | HOH668 |
| A | GLY158 |
| A | MLY161 |
| A | MLY161 |
| A | HOH507 |
| A | HOH507 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 326 |
| Chain | Residue |
| A | MLY9 |
| A | MLY185 |
| A | HOH677 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 327 |
| Chain | Residue |
| A | GLY22 |
| A | THR23 |
| A | TYR24 |
| A | ASP50 |
| A | TYR55 |
| A | LYS84 |
| A | HIS117 |
| A | SER166 |
| A | ASN167 |
| A | GLN190 |
| A | TYR216 |
| A | GLY217 |
| A | ALA218 |
| A | LEU219 |
| A | GLY220 |
| A | THR221 |
| A | GLN222 |
| A | TYR224 |
| A | LEU236 |
| A | ALA253 |
| A | ALA269 |
| A | GLN270 |
| A | GLU276 |
| A | GLU279 |
| A | ASN280 |
| A | MRD328 |
| A | HOH353 |
| A | HOH390 |
| A | HOH567 |
| A | HOH625 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD A 328 |
| Chain | Residue |
| A | TYR55 |
| A | HIS117 |
| A | TYR118 |
| A | TRP227 |
| A | PHE310 |
| A | NAD327 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeeckdaglVKSIGVSNF |
| Chain | Residue | Details |
| A | LEU151-PHE168 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHVDTAyayqvEeeIG |
| Chain | Residue | Details |
| A | GLY45-GLY62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of putative reductase (NP_038806.2) from Mus musculus at 1.18 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
