1QJG
Crystal structure of delta5-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004769 | molecular_function | steroid Delta-isomerase activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0004769 | molecular_function | steroid Delta-isomerase activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| C | 0004769 | molecular_function | steroid Delta-isomerase activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| D | 0004769 | molecular_function | steroid Delta-isomerase activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| E | 0004769 | molecular_function | steroid Delta-isomerase activity |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0008202 | biological_process | steroid metabolic process |
| E | 0016853 | molecular_function | isomerase activity |
| F | 0004769 | molecular_function | steroid Delta-isomerase activity |
| F | 0006629 | biological_process | lipid metabolic process |
| F | 0008202 | biological_process | steroid metabolic process |
| F | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1140 |
| Chain | Residue |
| B | HIS6 |
| B | ARG13 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EQU A 130 |
| Chain | Residue |
| A | TYR14 |
| A | ASN38 |
| A | PHE82 |
| A | PHE86 |
| A | ASP99 |
| A | MET112 |
| A | PHE116 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EQU B 130 |
| Chain | Residue |
| B | TYR14 |
| B | ASN38 |
| B | SER58 |
| B | PHE82 |
| B | VAL84 |
| B | VAL95 |
| B | ASP99 |
| B | MET112 |
| B | PHE116 |
| B | HOH2044 |
| D | ARG13 |
| D | ALA20 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU C 130 |
| Chain | Residue |
| C | TYR14 |
| C | ASN38 |
| C | PHE82 |
| C | PRO97 |
| C | ASP99 |
| C | MET112 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU D 130 |
| Chain | Residue |
| D | TYR14 |
| D | ASN38 |
| D | PHE86 |
| D | ASP99 |
| D | MET112 |
| D | PHE116 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EQU E 130 |
| Chain | Residue |
| C | ALA20 |
| C | HOH2006 |
| E | TYR14 |
| E | ASN38 |
| E | LEU61 |
| E | ASP99 |
| E | MET112 |
| E | PHE116 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU F 130 |
| Chain | Residue |
| F | TYR14 |
| F | ASN38 |
| F | PHE86 |
| F | ASP99 |
| F | MET112 |
| F | PHE116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"3480517","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| A | ASN38 | |
| A | PHE30 | |
| A | TYR14 | |
| A | ASP99 | |
| A | TYR55 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| B | ASN38 | |
| B | PHE30 | |
| B | TYR14 | |
| B | ASP99 | |
| B | TYR55 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| C | ASN38 | |
| C | PHE30 | |
| C | TYR14 | |
| C | ASP99 | |
| C | TYR55 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| D | ASN38 | |
| D | PHE30 | |
| D | TYR14 | |
| D | ASP99 | |
| D | TYR55 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| E | ASN38 | |
| E | PHE30 | |
| E | TYR14 | |
| E | ASP99 | |
| E | TYR55 |
| site_id | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| F | ASN38 | |
| F | PHE30 | |
| F | TYR14 | |
| F | ASP99 | |
| F | TYR55 |
