Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004769 | molecular_function | steroid delta-isomerase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016995 | molecular_function | cholesterol oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 510 |
| Chain | Residue |
| A | GLU40 |
| A | MET41 |
| A | TYR107 |
| A | ARG110 |
| A | GLY111 |
| A | GLY114 |
| A | GLY115 |
| A | ASN119 |
| A | GLY120 |
| A | GLY121 |
| A | MET122 |
| A | ILE218 |
| A | HIS248 |
| A | GLN249 |
| A | VAL250 |
| A | GLY288 |
| A | ALA289 |
| A | GLY290 |
| A | TYR446 |
| A | ASP474 |
| A | GLY475 |
| A | ASN485 |
| A | PRO486 |
| A | PHE487 |
| A | HOH541 |
| A | HOH553 |
| A | HOH568 |
| A | HOH575 |
| A | HOH608 |
| A | HOH625 |
| A | HOH639 |
| A | HOH696 |
| A | HOH710 |
| A | GLY17 |
| A | GLY19 |
| A | TYR20 |
| A | GLY21 |
| A | LEU39 |
| site_id | CAT |
| Number of Residues | 4 |
| Details | HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. THIS RESIDUE HAS BEEN MUTATED TO A GLUTAMINE. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE. |
| Chain | Residue |
| A | GLN447 |
| A | GLU361 |
| A | ASN485 |
| A | HOH541 |
Functional Information from PROSITE/UniProt
| site_id | PS00623 |
| Number of Residues | 24 |
| Details | GMC_OXRED_1 GMC oxidoreductases signature 1. GRgVGGGSlVNggmAvePkrsyfE |
| Chain | Residue | Details |
| A | GLY109-GLU132 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU361 | |
| A | GLN447 | |
| Chain | Residue | Details |
| A | TYR20 | |
| A | GLU40 | |
| A | GLY115 | |
| A | ASN119 | |
| A | VAL250 | |
| A | GLY475 | |
| A | PHE487 | |
| Chain | Residue | Details |
| A | TYR446 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1coy |
| Chain | Residue | Details |
| A | ASN485 | |
| A | GLU361 | |
| A | GLN447 | |
