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6YCT

Crystal structure of GcoA F169A_T296S bound to p-vanillin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EPE A 501
ChainResidue
ATRP107
ALEU111
ALEU147
AGLN151
AASP213
AHOH638

site_idAC2
Number of Residues9
Detailsbinding site for residue V55 A 502
ChainResidue
AALA246
AILE292
AALA295
ASER296
APHE395
AHEC503
AVAL241
ALEU244
AGLY245

site_idAC3
Number of Residues23
Detailsbinding site for residue HEC A 503
ChainResidue
AILE80
AILE81
AHIS88
AARG92
ALEU99
ATYR242
AALA246
AGLU249
APRO250
AILE292
ASER296
AARG298
ATYR321
AALA348
APHE349
AGLY350
AALA351
AHIS354
AALA355
ACYS356
AMET366
AV55502
AHOH698

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 site: {"evidences":[{"source":"PubMed","id":"29950589","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"29950589","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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