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2ZYQ

Crystal structure of the HsaC extradiol dioxygenase from M. tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0006629biological_processlipid metabolic process
A0006707biological_processcholesterol catabolic process
A0008198molecular_functionferrous iron binding
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0046872molecular_functionmetal ion binding
A0047071molecular_function3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity
A0051213molecular_functiondioxygenase activity
A0070723biological_processresponse to cholesterol
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0006629biological_processlipid metabolic process
B0006707biological_processcholesterol catabolic process
B0008198molecular_functionferrous iron binding
B0008202biological_processsteroid metabolic process
B0008203biological_processcholesterol metabolic process
B0016042biological_processlipid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0046872molecular_functionmetal ion binding
B0047071molecular_function3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity
B0051213molecular_functiondioxygenase activity
B0070723biological_processresponse to cholesterol
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A 301
ChainResidue
AHIS145
AHIS215
ATYR256
AGLU266
AHOH302
AHOH303

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 301
ChainResidue
BHOH303
BHOH304
BHIS145
BHIS215
BGLU266

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TAR B 302
ChainResidue
BPRO55
BGLY56
BLYS89
BARG106
BHOH318
BHOH630

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues22
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. GrHvndlmlsFYmkTPgGfdiE
ChainResidueDetails
AGLY245-GLU266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues230
DetailsDomain: {"description":"VOC 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues256
DetailsDomain: {"description":"VOC 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19300498","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mpy
ChainResidueDetails
AHIS200
ATYR256
AHIS247

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mpy
ChainResidueDetails
BHIS200
BTYR256
BHIS247

246704

PDB entries from 2025-12-24

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