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4DNJ

The crystal structures of 4-methoxybenzoate bound CYP199A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0006805biological_processxenobiotic metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0018690molecular_function4-methoxybenzoate monooxygenase (O-demethylating) activity
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AILE99
AARG303
AGLY353
APHE354
AGLY355
AHIS359
ACYS361
AVAL362
AGLY363
AALA367
AANN502
ALEU100
AHOH614
AHOH632
AHIS107
AARG111
AALA251
AGLY252
ATHR255
ATHR256
APHE301

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ANN A 502
ChainResidue
AARG94
ASER97
ALEU100
APHE185
ASER247
ASER250
AALA251
APHE301
AHEM501
AHOH645

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
ATYR180
AGLN206
AHOH778

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

218853

PDB entries from 2024-04-24

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