3PDJ
Crystal Structure of Human 11-beta-Hydroxysteroid Dehydrogenase 1 (11b-HSD1) in Complex with 4,4-Disubstituted Cyclohexylbenzamide Inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006706 | biological_process | steroid catabolic process |
| A | 0006713 | biological_process | glucocorticoid catabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| A | 0102196 | molecular_function | cortisol dehydrogenase (NADP+) activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006706 | biological_process | steroid catabolic process |
| B | 0006713 | biological_process | glucocorticoid catabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| B | 0102196 | molecular_function | cortisol dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 3PJ A 1 |
| Chain | Residue |
| A | THR124 |
| A | ALA223 |
| A | ALA226 |
| A | NAP293 |
| A | HOH324 |
| B | TYR280 |
| B | MET286 |
| B | HOH341 |
| A | LEU126 |
| A | SER170 |
| A | TYR177 |
| A | MET179 |
| A | TYR183 |
| A | LEU215 |
| A | GLY216 |
| A | THR222 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3PJ B 2 |
| Chain | Residue |
| A | TYR280 |
| B | NAP1 |
| B | THR124 |
| B | LEU126 |
| B | SER170 |
| B | TYR177 |
| B | TYR183 |
| B | LEU215 |
| B | GLY216 |
| B | ALA223 |
| B | ALA226 |
| B | MET233 |
| B | HOH301 |
| B | HOH302 |
| B | HOH365 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP B 1 |
| Chain | Residue |
| B | 3PJ2 |
| B | HOH4 |
| B | HOH14 |
| B | GLY41 |
| B | ALA42 |
| B | SER43 |
| B | LYS44 |
| B | GLY45 |
| B | ILE46 |
| B | ALA65 |
| B | ARG66 |
| B | SER67 |
| B | GLY91 |
| B | THR92 |
| B | MET93 |
| B | ASN119 |
| B | ILE121 |
| B | VAL168 |
| B | SER169 |
| B | SER170 |
| B | TYR183 |
| B | LYS187 |
| B | LEU215 |
| B | GLY216 |
| B | LEU217 |
| B | ILE218 |
| B | THR220 |
| B | THR222 |
| B | ALA223 |
| B | HOH296 |
| B | HOH302 |
| B | HOH329 |
| B | HOH330 |
| B | HOH338 |
| B | HOH357 |
| B | HOH359 |
| site_id | AC4 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 293 |
| Chain | Residue |
| A | HOH339 |
| A | 3PJ1 |
| A | HOH9 |
| A | GLY41 |
| A | SER43 |
| A | LYS44 |
| A | GLY45 |
| A | ILE46 |
| A | ALA65 |
| A | ARG66 |
| A | SER67 |
| A | THR92 |
| A | MET93 |
| A | ASN119 |
| A | ILE121 |
| A | VAL168 |
| A | SER169 |
| A | SER170 |
| A | TYR183 |
| A | LYS187 |
| A | LEU215 |
| A | GLY216 |
| A | LEU217 |
| A | ILE218 |
| A | THR220 |
| A | THR222 |
| A | ALA223 |
| A | HOH295 |
| A | HOH312 |
| A | HOH319 |
| A | HOH324 |
| A | HOH327 |
| A | HOH329 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkvaypmVaaYSASKFALdGFFsSIR |
| Chain | Residue | Details |
| A | SER170-ARG198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 74 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15513927","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17919905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18069989","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18485702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18553955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19217779","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15513927","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XU9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 267 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
