Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004769 | molecular_function | steroid delta-isomerase activity |
A | 0008202 | biological_process | steroid metabolic process |
A | 0016853 | molecular_function | isomerase activity |
B | 0004769 | molecular_function | steroid delta-isomerase activity |
B | 0008202 | biological_process | steroid metabolic process |
B | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
site_id | SIA |
Number of Residues | 4 |
Details | TYR A14 AND ASP A99 BOTH STABILIZE THE INTERMEDIATE BY FORMING HYDROGEN-BOND TO IT. ASP A38 TRANSFERS PROTON FROM C-4B TO C-6B. |
Chain | Residue |
A | TYR14 |
A | ASP38 |
A | ASP99 |
A | PHE101 |
site_id | SIB |
Number of Residues | 4 |
Details | TYR B14 AND ASP B99 BOTH STABILIZE THE INTERMEDIATE BY FORMING HYDROGEN-BOND TO IT. ASP B38 TRANSFERS PROTON FROM C-4B TO C-6B. |
Chain | Residue |
B | TYR14 |
B | ASP38 |
B | ASP99 |
B | PHE101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | TYR14 | |
B | TYR14 | |
Chain | Residue | Details |
A | ASP38 | |
B | ASP38 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP99 | |
B | ASP99 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1e3v |
Chain | Residue | Details |
A | ASP38 | |
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 | ASP38 | |
B | PHE30 | |
B | TYR14 | |
B | ASP99 | |
B | TYR55 | |