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2FR7

Crystal Structure of Cytochrome P450 CYP199A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006805biological_processxenobiotic metabolic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0018690molecular_function4-methoxybenzoate monooxygenase (O-demethylating) activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AILE99
AVAL298
APHE301
AARG303
ALEU326
AGLY353
APHE354
AGLY355
AVAL358
AHIS359
ACYS361
ALEU100
AVAL362
AALA367
AHOH507
AHOH512
AHOH552
AHOH732
AHIS107
AARG111
ALEU248
AALA251
AGLY252
ATHR255
ATHR256

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGVHMCVG
ChainResidueDetails
APHE354-GLY363

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22695988
ChainResidueDetails
AARG94
ASER247

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:18762195, ECO:0000269|PubMed:22695988
ChainResidueDetails
ACYS361

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AASP254
ATHR255

226707

PDB entries from 2024-10-30

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