5EPO
The three-dimensional structure of Clostridium absonum 7alpha-hydroxysteroid dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008206 | biological_process | bile acid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030573 | biological_process | bile acid catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008206 | biological_process | bile acid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030573 | biological_process | bile acid catabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0008206 | biological_process | bile acid metabolic process |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030573 | biological_process | bile acid catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0008206 | biological_process | bile acid metabolic process |
| D | 0016042 | biological_process | lipid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030573 | biological_process | bile acid catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | SER13 |
| A | ASN90 |
| A | TYR91 |
| A | GLY92 |
| A | ILE143 |
| A | TYR158 |
| A | LYS162 |
| A | PRO188 |
| A | GLY189 |
| A | ILE191 |
| A | THR193 |
| A | THR15 |
| A | ARG194 |
| A | ALA195 |
| A | ALA196 |
| A | TUD302 |
| A | HOH407 |
| A | HOH423 |
| A | HOH427 |
| A | HOH435 |
| A | HOH446 |
| A | HOH458 |
| A | ARG16 |
| A | HOH528 |
| A | GLY17 |
| A | ILE18 |
| A | ARG38 |
| A | PHE62 |
| A | ASN63 |
| A | ALA64 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue TUD A 302 |
| Chain | Residue |
| A | GLY93 |
| A | THR94 |
| A | THR145 |
| A | GLY147 |
| A | ARG155 |
| A | TYR158 |
| A | GLY189 |
| A | ALA196 |
| A | ASN199 |
| A | PHE204 |
| A | NAP301 |
| A | HOH421 |
| A | HOH443 |
| A | HOH476 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | LYS7 |
| A | GLY138 |
| A | ARG182 |
| A | ALA231 |
| A | SER232 |
| A | ASP233 |
| A | HOH418 |
| A | HOH501 |
| A | HOH563 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | SER13 |
| B | THR15 |
| B | ARG16 |
| B | GLY17 |
| B | ILE18 |
| B | ARG38 |
| B | LEU42 |
| B | PHE62 |
| B | ASN63 |
| B | ALA64 |
| B | ASN90 |
| B | TYR91 |
| B | GLY92 |
| B | ILE143 |
| B | TYR158 |
| B | LYS162 |
| B | PRO188 |
| B | GLY189 |
| B | ILE191 |
| B | THR193 |
| B | ARG194 |
| B | ALA195 |
| B | ALA196 |
| B | TUD302 |
| B | HOH401 |
| B | HOH416 |
| B | HOH423 |
| B | HOH437 |
| B | HOH451 |
| B | HOH464 |
| B | HOH478 |
| B | HOH511 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue TUD B 302 |
| Chain | Residue |
| B | GLY93 |
| B | THR94 |
| B | THR145 |
| B | GLY147 |
| B | ARG155 |
| B | TYR158 |
| B | GLY189 |
| B | ALA196 |
| B | ASN199 |
| B | PHE204 |
| B | NAP301 |
| B | HOH424 |
| B | HOH518 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | GLY138 |
| B | ARG182 |
| B | ALA231 |
| B | SER232 |
| B | ASP233 |
| B | HOH408 |
| B | HOH446 |
| B | HOH472 |
| B | HOH485 |
| B | LYS7 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | SER13 |
| C | THR15 |
| C | ARG16 |
| C | GLY17 |
| C | ILE18 |
| C | ARG38 |
| C | PHE62 |
| C | ASN63 |
| C | ALA64 |
| C | ASN90 |
| C | TYR91 |
| C | GLY92 |
| C | SER144 |
| C | TYR158 |
| C | LYS162 |
| C | PRO188 |
| C | GLY189 |
| C | ILE191 |
| C | THR193 |
| C | ARG194 |
| C | ALA195 |
| C | ALA196 |
| C | TUD302 |
| C | HOH431 |
| C | HOH450 |
| C | HOH465 |
| C | HOH470 |
| C | HOH492 |
| C | HOH503 |
| C | HOH528 |
| C | HOH531 |
| C | HOH565 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue TUD C 302 |
| Chain | Residue |
| C | GLY93 |
| C | THR94 |
| C | VAL96 |
| C | THR145 |
| C | GLY147 |
| C | ARG155 |
| C | TYR158 |
| C | GLY189 |
| C | ALA196 |
| C | ASN199 |
| C | NAP301 |
| C | HOH441 |
| C | HOH486 |
| C | HOH521 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | LYS7 |
| C | GLY138 |
| C | ARG182 |
| C | ALA231 |
| C | SER232 |
| C | ASP233 |
| C | HOH417 |
| C | HOH483 |
| C | HOH501 |
| site_id | AD1 |
| Number of Residues | 30 |
| Details | binding site for residue NAP D 301 |
| Chain | Residue |
| D | SER13 |
| D | THR15 |
| D | ARG16 |
| D | GLY17 |
| D | ILE18 |
| D | ARG38 |
| D | PHE62 |
| D | ASN63 |
| D | ALA64 |
| D | ASN90 |
| D | TYR91 |
| D | GLY92 |
| D | SER144 |
| D | TYR158 |
| D | LYS162 |
| D | GLY189 |
| D | ILE191 |
| D | THR193 |
| D | ARG194 |
| D | ALA195 |
| D | ALA196 |
| D | TUD302 |
| D | HOH407 |
| D | HOH418 |
| D | HOH472 |
| D | HOH505 |
| D | HOH508 |
| D | HOH523 |
| D | HOH529 |
| D | HOH536 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for residue TUD D 302 |
| Chain | Residue |
| D | GLY93 |
| D | THR94 |
| D | ASN95 |
| D | VAL96 |
| D | THR145 |
| D | GLY147 |
| D | TYR158 |
| D | GLY189 |
| D | ALA196 |
| D | ASN199 |
| D | MET200 |
| D | PHE204 |
| D | NAP301 |
| D | HOH434 |
| D | HOH449 |
| D | HOH504 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL D 303 |
| Chain | Residue |
| D | ILE86 |
| D | GLY138 |
| D | ARG182 |
| D | ALA231 |
| D | ASP233 |
| D | HOH401 |
| D | HOH428 |
| D | HOH446 |
| D | HOH450 |
| D | HOH518 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0AET8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26961171","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EPO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"P0AET8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






