3C3U
Crystal structure of AKR1C1 in complex with NADP and 3,5-dichlorosalicylic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001523 | biological_process | retinoid metabolic process |
A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
A | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
A | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006693 | biological_process | prostaglandin metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0007586 | biological_process | digestion |
A | 0008206 | biological_process | bile acid metabolic process |
A | 0015721 | biological_process | bile acid and bile salt transport |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
A | 0030283 | molecular_function | testosterone dehydrogenase [NAD(P)+] activity |
A | 0030299 | biological_process | intestinal cholesterol absorption |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0031406 | molecular_function | carboxylic acid binding |
A | 0032052 | molecular_function | bile acid binding |
A | 0033703 | molecular_function | 3beta-hydroxy-5beta-steroid dehydrogenase activity |
A | 0033764 | molecular_function | steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0035410 | molecular_function | dihydrotestosterone 17-beta-dehydrogenase activity |
A | 0042448 | biological_process | progesterone metabolic process |
A | 0042574 | biological_process | retinal metabolic process |
A | 0042632 | biological_process | cholesterol homeostasis |
A | 0044597 | biological_process | daunorubicin metabolic process |
A | 0044598 | biological_process | doxorubicin metabolic process |
A | 0046683 | biological_process | response to organophosphorus |
A | 0047006 | molecular_function | 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity |
A | 0047023 | molecular_function | androsterone dehydrogenase activity |
A | 0047024 | molecular_function | 5alpha-androstane-3beta,17beta-diol dehydrogenase activity |
A | 0047042 | molecular_function | androsterone dehydrogenase (B-specific) activity |
A | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase activity |
A | 0047045 | molecular_function | testosterone 17-beta-dehydrogenase (NADP+) activity |
A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
A | 0047115 | molecular_function | trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity |
A | 0047718 | molecular_function | indanol dehydrogenase activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071395 | biological_process | cellular response to jasmonic acid stimulus |
A | 2000379 | biological_process | positive regulation of reactive oxygen species metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 324 |
Chain | Residue |
A | GLU133 |
A | HIS248 |
A | GLU292 |
A | HOH673 |
site_id | AC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP A 350 |
Chain | Residue |
A | HIS117 |
A | SER166 |
A | ASN167 |
A | GLN190 |
A | TYR216 |
A | SER217 |
A | ALA218 |
A | LEU219 |
A | GLY220 |
A | SER221 |
A | HIS222 |
A | LEU236 |
A | ALA253 |
A | LEU268 |
A | LYS270 |
A | SER271 |
A | TYR272 |
A | ARG276 |
A | GLN279 |
A | ASN280 |
A | LEU306 |
A | HOH364 |
A | HOH424 |
A | HOH428 |
A | HOH436 |
A | HOH483 |
A | HOH678 |
A | GLY22 |
A | THR23 |
A | TYR24 |
A | ASP50 |
A | TYR55 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C2U A 351 |
Chain | Residue |
A | TYR24 |
A | LEU54 |
A | TYR55 |
A | TRP86 |
A | HIS117 |
A | HIS222 |
A | TRP227 |
A | LEU308 |
Functional Information from PROSITE/UniProt
site_id | PS00062 |
Number of Residues | 18 |
Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. VekckdaglAKSIGVSNF |
Chain | Residue | Details |
A | VAL151-PHE168 |
site_id | PS00063 |
Number of Residues | 16 |
Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKSYNeqRIrQNvQV |
Chain | Residue | Details |
A | LEU268-VAL283 |
site_id | PS00798 |
Number of Residues | 18 |
Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHIDSAhlynnEeqVG |
Chain | Residue | Details |
A | GLY45-GLY62 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | TYR55 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 |
Chain | Residue | Details |
A | GLY20 | |
A | ASP50 | |
A | SER166 | |
A | GLN190 | |
A | TYR216 | |
A | LYS270 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR24 | |
A | HIS222 | |
A | TRP227 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS117 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000250 |
Chain | Residue | Details |
A | LEU54 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
Chain | Residue | Details |
A | LYS84 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: May be involved in the mediating step between the transformation of progesterone and the release of the cofactor |
Chain | Residue | Details |
A | HIS222 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS84 | |
A | HIS117 | |
A | ASP50 | |
A | TYR55 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS84 | |
A | TYR55 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 858 |
Chain | Residue | Details |
A | ASP50 | electrostatic stabiliser |
A | TYR55 | proton shuttle (general acid/base) |
A | LYS84 | modifies pKa |
A | HIS117 | proton shuttle (general acid/base) |