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 | 0006706 | biological_process | steroid catabolic process |
A | 0008202 | biological_process | steroid metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030324 | biological_process | lung development |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
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 activity |
B | 0005496 | molecular_function | steroid binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006706 | biological_process | steroid catabolic process |
B | 0008202 | biological_process | steroid metabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030324 | biological_process | lung development |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
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 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 | 534 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
A | GLU25-LYS292 | |
B | GLU25-LYS292 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR183 | |
B | TYR183 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 |
Chain | Residue | Details |
A | GLY41 | |
B | ILE218 | |
A | THR92 | |
A | ASN119 | |
A | TYR183 | |
A | ILE218 | |
B | GLY41 | |
B | THR92 | |
B | ASN119 | |
B | TYR183 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0007744|PDB:1XU7, ECO:0007744|PDB:1XU9 |
Chain | Residue | Details |
A | SER170 | |
B | SER170 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN123 | |
A | ASN162 | |
B | ASN123 | |
B | ASN162 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN207 | |
B | ASN207 |