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6HQT

Crystal structure of GcoA F169V bound to syringol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0019439biological_processobsolete aromatic compound catabolic process
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue HEM A 501
ChainResidue
AILE80
AILE292
ATHR296
AARG298
ATYR321
AALA348
APHE349
AGLY350
AALA351
AHIS354
AALA355
AILE81
ACYS356
AMET366
A3DM502
AHOH714
AHIS88
AARG92
ALEU99
ATYR242
AALA246
AGLU249
APRO250

site_idAC2
Number of Residues12
Detailsbinding site for residue 3DM A 502
ChainResidue
APHE75
AILE81
AVAL169
AVAL241
ALEU244
AGLY245
AALA246
AILE292
AALA295
ATHR296
APHE395
AHEM501

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGNHACAG
ChainResidueDetails
APHE349-GLY358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:29950589
ChainResidueDetails
AARG92
AVAL241
AGLY245
AARG298
ATYR321
AALA351
AHIS354
AHIS88

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:29950589
ChainResidueDetails
ACYS356

219869

PDB entries from 2024-05-15

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