2ZYQ
Crystal structure of the HsaC extradiol dioxygenase from M. tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047071 | molecular_function | 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0070723 | biological_process | response to cholesterol |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047071 | molecular_function | 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0070723 | biological_process | response to cholesterol |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A 301 |
| Chain | Residue |
| A | HIS145 |
| A | HIS215 |
| A | TYR256 |
| A | GLU266 |
| A | HOH302 |
| A | HOH303 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 301 |
| Chain | Residue |
| B | HOH303 |
| B | HOH304 |
| B | HIS145 |
| B | HIS215 |
| B | GLU266 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TAR B 302 |
| Chain | Residue |
| B | PRO55 |
| B | GLY56 |
| B | LYS89 |
| B | ARG106 |
| B | HOH318 |
| B | HOH630 |
Functional Information from PROSITE/UniProt
| site_id | PS00082 |
| Number of Residues | 22 |
| Details | EXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. GrHvndlmlsFYmkTPgGfdiE |
| Chain | Residue | Details |
| A | GLY245-GLU266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS145 | |
| A | GLU266 | |
| B | HIS145 | |
| B | GLU266 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19300498 |
| Chain | Residue | Details |
| A | HIS200 | |
| A | HIS215 | |
| A | ASP250 | |
| A | TYR256 | |
| B | HIS200 | |
| B | HIS215 | |
| B | ASP250 | |
| B | TYR256 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mpy |
| Chain | Residue | Details |
| A | HIS200 | |
| A | TYR256 | |
| A | HIS247 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mpy |
| Chain | Residue | Details |
| B | HIS200 | |
| B | TYR256 | |
| B | HIS247 |
