##gff-version 3
Q05556	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000051674;Note=Cytochrome P450 2A11	
Q05556	UniProtKB	Binding site	439	439	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q05556	UniProtKB	Modified residue	379	379	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64458	
Q05556	UniProtKB	Mutagenesis	62	63	.	.	.	Note=No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation%3B when associated with L-104%3B V-117 and S-120. RD->SE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8074681;Dbxref=PMID:8074681	
Q05556	UniProtKB	Mutagenesis	104	104	.	.	.	Note=No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation%3B when associated with 62-SE-63%3B V-117 and S-120. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8074681;Dbxref=PMID:8074681	
Q05556	UniProtKB	Mutagenesis	117	117	.	.	.	Note=No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation%3B when associated with 62-SE-63%3B L-104 and S-120. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8074681;Dbxref=PMID:8074681	
Q05556	UniProtKB	Mutagenesis	120	120	.	.	.	Note=No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation%3B when associated with 62-SE-63%3B L-104 and V-117. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8074681;Dbxref=PMID:8074681	
Q05556	UniProtKB	Mutagenesis	372	372	.	.	.	Note=Significant increase in the rate of hydroxylation of testosterone%2C but not of coumarin. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8074681;Dbxref=PMID:8074681