2ZI8
Crystal structure of the HsaC extradiol dioxygenase from M. tuberculosis in complex with 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (DHSA)
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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008203 | biological_process | cholesterol metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0019439 | biological_process | obsolete aromatic compound 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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
B | 0008198 | molecular_function | ferrous iron binding |
B | 0008203 | biological_process | cholesterol metabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0019439 | biological_process | obsolete aromatic compound 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 701 |
Chain | Residue |
A | HIS145 |
A | HIS215 |
A | TYR256 |
A | GLU266 |
A | SDT702 |
A | HOH839 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B 701 |
Chain | Residue |
B | SDT702 |
B | HOH887 |
B | HOH944 |
B | HIS145 |
B | HIS215 |
B | GLU266 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SDT A 702 |
Chain | Residue |
A | HIS145 |
A | MET172 |
A | HIS200 |
A | VAL214 |
A | HIS215 |
A | HIS247 |
A | ASN249 |
A | ASP250 |
A | TYR256 |
A | GLU266 |
A | VAL287 |
A | FE2701 |
A | HOH736 |
A | HOH839 |
A | HOH842 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SDT B 702 |
Chain | Residue |
B | MET172 |
B | PHE192 |
B | HIS200 |
B | VAL214 |
B | HIS215 |
B | HIS247 |
B | ASN249 |
B | ASP250 |
B | TYR256 |
B | VAL287 |
B | FE2701 |
B | HOH783 |
B | HOH808 |
B | HOH887 |
B | HOH921 |
B | HOH943 |
B | HOH944 |
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 |