4IJW
Crystal structure of 11b-HSD1 double mutant (L262R, F278E) in complex with 3-[1-(4-chlorophenyl)cyclopropyl]-8-cyclopropyl[1,2,4]triazolo[4,3-a]pyridine
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 |
D | 0005496 | molecular_function | steroid binding |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0005789 | cellular_component | endoplasmic reticulum membrane |
D | 0006706 | biological_process | steroid catabolic process |
D | 0008202 | biological_process | steroid metabolic process |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0030324 | biological_process | lung development |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
D | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
D | 0050661 | molecular_function | NADP binding |
D | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
D | 0102196 | molecular_function | cortisol dehydrogenase activity |
E | 0005496 | molecular_function | steroid binding |
E | 0005783 | cellular_component | endoplasmic reticulum |
E | 0005789 | cellular_component | endoplasmic reticulum membrane |
E | 0006706 | biological_process | steroid catabolic process |
E | 0008202 | biological_process | steroid metabolic process |
E | 0016020 | cellular_component | membrane |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0030324 | biological_process | lung development |
E | 0042803 | molecular_function | protein homodimerization activity |
E | 0043231 | cellular_component | intracellular membrane-bounded organelle |
E | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
E | 0050661 | molecular_function | NADP binding |
E | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
E | 0102196 | molecular_function | cortisol dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAP A 301 |
Chain | Residue |
A | GLY41 |
A | MET93 |
A | GLU94 |
A | ASN119 |
A | ILE121 |
A | VAL168 |
A | SER169 |
A | SER170 |
A | TYR183 |
A | LYS187 |
A | LEU215 |
A | SER43 |
A | GLY216 |
A | ILE218 |
A | THR220 |
A | THR222 |
A | ALA223 |
A | 1EQ302 |
A | HOH401 |
A | HOH436 |
A | LYS44 |
A | GLY45 |
A | ILE46 |
A | ALA65 |
A | ARG66 |
A | SER67 |
A | THR92 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1EQ A 302 |
Chain | Residue |
A | ILE121 |
A | SER170 |
A | TYR177 |
A | PRO178 |
A | TYR183 |
A | GLY216 |
A | LEU217 |
A | ALA223 |
A | VAL231 |
A | NAP301 |
B | TYR284 |
site_id | AC3 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP B 301 |
Chain | Residue |
B | GLY41 |
B | ALA42 |
B | SER43 |
B | LYS44 |
B | GLY45 |
B | ILE46 |
B | ALA65 |
B | ARG66 |
B | SER67 |
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 | 1EQ302 |
B | HOH408 |
B | HOH420 |
B | HOH422 |
B | HOH426 |
B | HOH438 |
B | HOH445 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 1EQ B 302 |
Chain | Residue |
A | TYR284 |
B | THR124 |
B | SER170 |
B | TYR177 |
B | PRO178 |
B | VAL180 |
B | TYR183 |
B | GLY216 |
B | LEU217 |
B | VAL227 |
B | VAL231 |
B | MET233 |
B | NAP301 |
site_id | AC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP D 301 |
Chain | Residue |
D | TYR183 |
D | LYS187 |
D | LEU215 |
D | GLY216 |
D | ILE218 |
D | THR220 |
D | THR222 |
D | ALA223 |
D | 1EQ302 |
D | HOH402 |
D | HOH404 |
D | HOH405 |
D | HOH436 |
D | HOH437 |
D | GLY41 |
D | ALA42 |
D | SER43 |
D | LYS44 |
D | GLY45 |
D | ILE46 |
D | ALA65 |
D | ARG66 |
D | SER67 |
D | THR92 |
D | MET93 |
D | ASN119 |
D | ILE121 |
D | VAL168 |
D | SER169 |
D | SER170 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1EQ D 302 |
Chain | Residue |
D | ILE121 |
D | SER170 |
D | TYR177 |
D | PRO178 |
D | MET179 |
D | TYR183 |
D | GLY216 |
D | LEU217 |
D | ALA223 |
D | NAP301 |
E | TYR284 |
site_id | AC7 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP E 301 |
Chain | Residue |
E | GLY41 |
E | SER43 |
E | LYS44 |
E | GLY45 |
E | ILE46 |
E | ALA65 |
E | ARG66 |
E | SER67 |
E | THR92 |
E | MET93 |
E | ASN119 |
E | HIS120 |
E | ILE121 |
E | VAL168 |
E | SER169 |
E | SER170 |
E | TYR183 |
E | LYS187 |
E | LEU215 |
E | GLY216 |
E | LEU217 |
E | ILE218 |
E | THR220 |
E | THR222 |
E | ALA223 |
E | 1EQ302 |
E | HOH406 |
E | HOH410 |
E | HOH412 |
E | HOH413 |
E | HOH433 |
E | HOH439 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1EQ E 302 |
Chain | Residue |
E | ILE121 |
E | SER170 |
E | TYR177 |
E | PRO178 |
E | TYR183 |
E | GLY216 |
E | LEU217 |
E | ALA223 |
E | VAL231 |
E | NAP301 |
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 | 1068 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
A | GLU25-LYS292 | |
B | GLU25-LYS292 | |
D | GLU25-LYS292 | |
E | GLU25-LYS292 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR183 | |
B | TYR183 | |
D | TYR183 | |
E | TYR183 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
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 | |
D | GLY41 | |
D | THR92 | |
D | ASN119 | |
D | TYR183 | |
D | ILE218 | |
E | GLY41 | |
E | THR92 | |
E | ASN119 | |
E | TYR183 | |
A | THR92 | |
E | ILE218 | |
A | ASN119 | |
A | TYR183 | |
A | ILE218 | |
B | GLY41 | |
B | THR92 | |
B | ASN119 | |
B | TYR183 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0007744|PDB:1XU7, ECO:0007744|PDB:1XU9 |
Chain | Residue | Details |
A | SER170 | |
B | SER170 | |
D | SER170 | |
E | SER170 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN123 | |
A | ASN162 | |
B | ASN123 | |
B | ASN162 | |
D | ASN123 | |
D | ASN162 | |
E | ASN123 | |
E | ASN162 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN207 | |
B | ASN207 | |
D | ASN207 | |
E | ASN207 |