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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EQU A 132 |
| Chain | Residue |
| A | TYR16 |
| A | ASN40 |
| A | MET90 |
| A | LEU99 |
| A | ASN103 |
| A | TRP120 |
| B | TRP92 |
| B | ASN93 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 133 |
| Chain | Residue |
| A | ASN93 |
| A | HOH169 |
| B | VAL91 |
| B | TRP92 |
| B | EQU132 |
| B | HOH140 |
| B | HOH239 |
| A | TRP92 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 134 |
| Chain | Residue |
| A | GLU39 |
| A | PRO46 |
| A | HOH150 |
| A | HOH198 |
| B | ASP34 |
| B | GLY49 |
| B | ARG50 |
| B | HOH211 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA A 135 |
| Chain | Residue |
| A | THR5 |
| A | ALA6 |
| A | HIS78 |
| A | HOH171 |
| A | HOH203 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EQU B 132 |
| Chain | Residue |
| A | ASN93 |
| A | GOL133 |
| B | TYR16 |
| B | ASN40 |
| B | MET90 |
| B | LEU99 |
| B | ASN103 |
| B | TRP120 |
| B | HOH243 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11007792","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| A | ASN103 | |
| A | ASN40 | |
| A | TYR32 | |
| A | TYR16 | |
| A | TYR57 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1e3v |
| Chain | Residue | Details |
| B | ASN103 | |
| B | ASN40 | |
| B | TYR32 | |
| B | TYR16 | |
| B | TYR57 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| A | TYR16 | proton acceptor, proton donor |
| A | ASN40 | proton acceptor, proton donor |
| A | ASP100 | electrostatic stabiliser |
| A | ASN103 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| B | TYR16 | proton acceptor, proton donor |
| B | ASN40 | proton acceptor, proton donor |
| B | ASP100 | electrostatic stabiliser |
| B | ASN103 | electrostatic stabiliser |
