3BUR
Crystal structure of Delta(4)-3-ketosteroid 5-beta-reductase in complex with NADP and TESTOSTERONE. RESOLUTION: 1.62 A.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006066 | biological_process | alcohol metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006699 | biological_process | bile acid biosynthetic process |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0007586 | biological_process | digestion |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008207 | biological_process | C21-steroid hormone metabolic process |
| A | 0008209 | biological_process | androgen metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016229 | molecular_function | steroid dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030573 | biological_process | bile acid catabolic process |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| A | 0042445 | biological_process | hormone metabolic process |
| A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
| A | 0047787 | molecular_function | Delta4-3-oxosteroid 5beta-reductase activity |
| B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006066 | biological_process | alcohol metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006699 | biological_process | bile acid biosynthetic process |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0007586 | biological_process | digestion |
| B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008207 | biological_process | C21-steroid hormone metabolic process |
| B | 0008209 | biological_process | androgen metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016229 | molecular_function | steroid dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030573 | biological_process | bile acid catabolic process |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0042445 | biological_process | hormone metabolic process |
| B | 0047086 | molecular_function | ketosteroid monooxygenase activity |
| B | 0047787 | molecular_function | Delta4-3-oxosteroid 5beta-reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP B 327 |
| Chain | Residue |
| B | GLY24 |
| B | SER220 |
| B | PRO221 |
| B | LEU222 |
| B | GLY223 |
| B | THR224 |
| B | SER225 |
| B | LEU239 |
| B | ALA256 |
| B | ILE271 |
| B | PRO272 |
| B | THR25 |
| B | LYS273 |
| B | SER274 |
| B | PHE275 |
| B | ARG279 |
| B | GLU282 |
| B | ASN283 |
| B | HOH1062 |
| B | HOH1067 |
| B | HOH1162 |
| B | HOH1367 |
| B | TYR26 |
| B | HOH1410 |
| B | HOH1476 |
| B | ASP53 |
| B | TYR58 |
| B | SER169 |
| B | ASN170 |
| B | GLN193 |
| B | TYR219 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP A 328 |
| Chain | Residue |
| A | GLY24 |
| A | THR25 |
| A | TYR26 |
| A | ASP53 |
| A | TYR58 |
| A | LYS87 |
| A | SER169 |
| A | ASN170 |
| A | GLN193 |
| A | TYR219 |
| A | SER220 |
| A | PRO221 |
| A | LEU222 |
| A | GLY223 |
| A | THR224 |
| A | SER225 |
| A | LEU239 |
| A | ALA256 |
| A | ILE271 |
| A | PRO272 |
| A | LYS273 |
| A | SER274 |
| A | PHE275 |
| A | ARG279 |
| A | GLU282 |
| A | ASN283 |
| A | HOH1042 |
| A | HOH1082 |
| A | HOH1229 |
| A | HOH1252 |
| A | HOH1315 |
| A | HOH1486 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TES A 339 |
| Chain | Residue |
| A | TYR26 |
| A | ILE57 |
| A | TRP89 |
| A | TYR132 |
| A | SER225 |
| A | ARG226 |
| A | ASN227 |
| A | TRP230 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TES B 340 |
| Chain | Residue |
| B | TYR26 |
| B | ILE57 |
| B | TRP89 |
| B | TYR132 |
| B | THR224 |
| B | SER225 |
| B | ARG226 |
| B | ASN227 |
| B | TRP230 |
| B | HOH1367 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 329 |
| Chain | Residue |
| A | GLU103 |
| A | ARG107 |
| A | LEU111 |
| B | ASP129 |
| B | HOH1078 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 330 |
| Chain | Residue |
| B | THR224 |
| B | SER225 |
| B | ARG226 |
| B | HOH1457 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 331 |
| Chain | Residue |
| A | ARG134 |
| A | ILE229 |
| A | TRP230 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 332 |
| Chain | Residue |
| A | THR224 |
| A | SER225 |
| A | ARG226 |
| A | LEU239 |
| A | HOH1486 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 333 |
| Chain | Residue |
| A | HOH1131 |
| B | MET97 |
| B | PRO100 |
| B | THR101 |
| B | ARG104 |
| A | ASP112 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 334 |
| Chain | Residue |
| A | SER225 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 335 |
| Chain | Residue |
| A | LEU106 |
| A | ARG107 |
| A | GLN110 |
| A | LEU111 |
| A | HOH1032 |
| B | LEU243 |
| B | ASP298 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 336 |
| Chain | Residue |
| B | ARG279 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 337 |
| Chain | Residue |
| A | ARG99 |
| A | GLU103 |
| A | LEU162 |
| A | HOH1123 |
| B | TYR56 |
| B | ARG104 |
| B | ASP129 |
| B | HOH1339 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 338 |
| Chain | Residue |
| A | ARG279 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeackdaglVKSLGVSNF |
| Chain | Residue | Details |
| A | MET154-PHE171 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSFNleRIkENfQI |
| Chain | Residue | Details |
| A | ILE271-ILE286 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDGAyiyqnEheVG |
| Chain | Residue | Details |
| A | GLY48-GLY65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18407998","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18624455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18848863","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19075558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19515843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22437839","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| 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 | TYR58 | |
| A | GLU120 | |
| A | LYS87 | |
| A | ASP53 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | TYR58 | |
| B | GLU120 | |
| B | LYS87 | |
| B | ASP53 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | TYR58 | |
| A | LYS87 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | TYR58 | |
| B | LYS87 |
