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6J94

Crystal structure of CYP97A3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue HEM A 601
ChainResidue
ALYS174
AGLN440
ALEU444
AARG446
APRO508
APHE509
AGLY510
AARG514
ALYS515
ACYS516
AGLY518
ATRP197
APHE521
AALA522
AASN526
AHOH730
AHOH764
AHOH772
AHOH827
AHOH878
AARG201
AALA377
AGLY378
ATHR381
ASER382
AVAL385
ALEU435

site_idAC2
Number of Residues26
Detailsbinding site for residue HEM B 601
ChainResidue
BLYS174
BTRP197
BARG201
BALA377
BGLY378
BTHR381
BVAL385
BGLN440
BLEU444
BARG446
BPRO508
BPHE509
BGLY510
BARG514
BLYS515
BCYS516
BILE517
BGLY518
BPHE521
BALA522
BHOH702
BHOH720
BHOH759
BHOH823
BHOH855
BHOH887

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGPRKCIG
ChainResidueDetails
APHE509-GLY518

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:32513704
ChainResidueDetails
ACYS516
BCYS516

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PDB entries from 2024-07-24

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