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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EQU A 200 |
| Chain | Residue |
| A | TYR16 |
| A | ASN40 |
| A | GLY60 |
| A | MET90 |
| A | TRP92 |
| A | LEU99 |
| A | ASP103 |
| A | MET116 |
| A | TRP120 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU B 200 |
| Chain | Residue |
| B | TYR16 |
| B | ASN40 |
| B | MET90 |
| B | ASP103 |
| B | MET116 |
| B | TRP120 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EQU C 200 |
| Chain | Residue |
| C | TYR16 |
| C | ASN40 |
| C | GLY60 |
| C | MET90 |
| C | TRP92 |
| C | LEU99 |
| C | ASP103 |
| C | MET116 |
| C | TRP120 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EQU D 200 |
| Chain | Residue |
| D | TYR16 |
| D | ASN40 |
| D | MET90 |
| D | ASP103 |
| D | MET116 |
| D | TRP120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11007792","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| 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 | VAL104 | electrostatic stabiliser |
| A | PHE107 | 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 | VAL104 | electrostatic stabiliser |
| B | PHE107 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| C | TYR16 | proton acceptor, proton donor |
| C | ASN40 | proton acceptor, proton donor |
| C | VAL104 | electrostatic stabiliser |
| C | PHE107 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 349 |
| Chain | Residue | Details |
| D | TYR16 | proton acceptor, proton donor |
| D | ASN40 | proton acceptor, proton donor |
| D | VAL104 | electrostatic stabiliser |
| D | PHE107 | electrostatic stabiliser |
