1XU9
Crystal Structure of the Interface Closed Conformation of 11b-hydroxysteroid dehydrogenase isozyme 1
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 |
C | 0005496 | molecular_function | steroid binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005789 | cellular_component | endoplasmic reticulum membrane |
C | 0006706 | biological_process | steroid catabolic process |
C | 0008202 | biological_process | steroid metabolic process |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0030324 | biological_process | lung development |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
C | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
C | 0050661 | molecular_function | NADP binding |
C | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
C | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE NDP A 1 |
Chain | Residue |
A | CPS5 |
A | SER67 |
A | THR92 |
A | MET93 |
A | ASN119 |
A | ILE121 |
A | VAL168 |
A | SER169 |
A | SER170 |
A | TYR183 |
A | LYS187 |
A | GLY41 |
A | LEU215 |
A | GLY216 |
A | LEU217 |
A | ILE218 |
A | THR220 |
A | THR222 |
A | ALA223 |
A | HOH1507 |
A | HOH1520 |
A | HOH1533 |
A | ALA42 |
A | HOH1581 |
A | HOH1631 |
A | HOH1657 |
A | HOH1662 |
A | HOH1685 |
A | HOH1798 |
A | HOH1974 |
A | SER43 |
A | LYS44 |
A | GLY45 |
A | ILE46 |
A | ALA65 |
A | ARG66 |
site_id | AC2 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE NDP B 2 |
Chain | Residue |
B | CPS6 |
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 | HOH1513 |
B | HOH1527 |
B | HOH1568 |
B | HOH1590 |
B | HOH1606 |
B | HOH1620 |
B | HOH1626 |
B | HOH1762 |
B | HOH1797 |
B | HOH1892 |
site_id | AC3 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NDP C 3 |
Chain | Residue |
C | HOH295 |
C | HOH314 |
C | HOH329 |
C | HOH341 |
C | HOH361 |
C | HOH428 |
C | HOH457 |
C | HOH506 |
C | GLY41 |
C | ALA42 |
C | SER43 |
C | LYS44 |
C | GLY45 |
C | ILE46 |
C | ALA65 |
C | ARG66 |
C | SER67 |
C | THR92 |
C | MET93 |
C | ASN119 |
C | HIS120 |
C | ILE121 |
C | VAL168 |
C | SER169 |
C | SER170 |
C | TYR183 |
C | LYS187 |
C | LEU215 |
C | GLY216 |
C | LEU217 |
C | ILE218 |
C | THR220 |
C | THR222 |
C | ALA223 |
C | CPS293 |
site_id | AC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NDP D 4 |
Chain | Residue |
D | GLY41 |
D | SER43 |
D | GLY45 |
D | ILE46 |
D | ALA65 |
D | ARG66 |
D | SER67 |
D | THR92 |
D | MET93 |
D | ASN119 |
D | ILE121 |
D | VAL168 |
D | SER169 |
D | SER170 |
D | TYR183 |
D | LYS187 |
D | LEU215 |
D | GLY216 |
D | LEU217 |
D | ILE218 |
D | THR220 |
D | THR222 |
D | ALA223 |
D | CPS293 |
D | HOH304 |
D | HOH306 |
D | HOH307 |
D | HOH309 |
D | HOH330 |
D | HOH387 |
D | HOH427 |
D | HOH497 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CPS A 5 |
Chain | Residue |
A | NDP1 |
A | LEU171 |
A | TYR177 |
A | TYR183 |
A | LEU217 |
A | GLN234 |
A | SER261 |
A | THR264 |
A | HOH1505 |
A | HOH1594 |
A | HOH1883 |
A | HOH2876 |
B | TYR280 |
B | SER283 |
B | TYR284 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CPS B 6 |
Chain | Residue |
A | TYR280 |
A | SER283 |
B | NDP2 |
B | ILE121 |
B | LEU171 |
B | TYR177 |
B | TYR183 |
B | LEU217 |
B | ALA223 |
B | MET233 |
B | GLN234 |
B | THR264 |
B | HOH1517 |
B | HOH1554 |
B | HOH1803 |
C | TRP263 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CPS C 293 |
Chain | Residue |
C | NDP3 |
C | ILE121 |
C | LEU171 |
C | TYR177 |
C | TYR183 |
C | LEU217 |
C | SER261 |
C | TRP263 |
C | THR264 |
C | HOH294 |
C | HOH304 |
C | HOH376 |
C | HOH401 |
C | HOH462 |
D | TYR280 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CPS D 293 |
Chain | Residue |
C | TYR280 |
D | NDP4 |
D | ILE121 |
D | LEU171 |
D | TYR177 |
D | TYR183 |
D | LEU217 |
D | SER261 |
D | TRP263 |
D | THR264 |
D | HOH295 |
D | HOH299 |
D | HOH322 |
D | HOH355 |
D | HOH392 |
D | HOH570 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MES A 293 |
Chain | Residue |
A | TYR177 |
A | PRO178 |
A | VAL227 |
A | SER228 |
A | VAL231 |
A | HOH2133 |
A | HOH2268 |
B | TYR284 |
B | ARG288 |
B | HOH2780 |
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 | |
C | GLU25-LYS292 | |
D | GLU25-LYS292 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR183 | |
B | TYR183 | |
C | TYR183 | |
D | 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 | |
C | GLY41 | |
C | THR92 | |
C | ASN119 | |
C | TYR183 | |
C | ILE218 | |
D | GLY41 | |
D | THR92 | |
D | ASN119 | |
D | TYR183 | |
A | THR92 | |
D | 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 | |
C | SER170 | |
D | 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 | |
C | ASN123 | |
C | ASN162 | |
D | ASN123 | |
D | 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 | |
C | ASN207 | |
D | ASN207 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS174 |
site_id | CSA10 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS187 | |
B | SER170 | |
B | TYR183 | |
B | ASN143 |
site_id | CSA11 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS187 | |
C | SER170 | |
C | TYR183 | |
C | ASN143 |
site_id | CSA12 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS187 | |
D | SER170 | |
D | TYR183 | |
D | ASN143 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS187 | |
A | VAL180 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS187 | |
B | VAL180 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS187 | |
C | VAL180 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS187 | |
D | VAL180 |
site_id | CSA17 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS187 | |
A | TYR183 |
site_id | CSA18 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS187 | |
B | TYR183 |
site_id | CSA19 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS187 | |
C | TYR183 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS174 |
site_id | CSA20 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS187 | |
D | TYR183 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS174 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS174 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS187 | |
A | SER170 | |
A | TYR183 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LYS187 | |
B | SER170 | |
B | TYR183 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LYS187 | |
C | SER170 | |
C | TYR183 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LYS187 | |
D | SER170 | |
D | TYR183 |
site_id | CSA9 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LYS187 | |
A | SER170 | |
A | TYR183 | |
A | ASN143 |