2H7S

L244A mutant of Cytochrome P450cam

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006707	biological_process	cholesterol catabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0018683	molecular_function	camphor 5-monooxygenase activity
A	0019383	biological_process	(+)-camphor catabolic process
A	0020037	molecular_function	heme binding
A	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0006707	biological_process	cholesterol catabolic process
C	0008395	molecular_function	steroid hydroxylase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0018683	molecular_function	camphor 5-monooxygenase activity
C	0019383	biological_process	(+)-camphor catabolic process
C	0020037	molecular_function	heme binding
C	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A 415

Chain	Residue
A	PRO100
A	ASP297
A	ARG299
A	GLN322
A	THR349
A	PHE350
A	GLY351
A	HIS355
A	CYS357
A	LEU358
A	GLY359
A	THR101
A	ALA363
A	HOH492
A	HOH518
A	GLN108
A	ARG112
A	VAL119
A	GLY248
A	THR252
A	VAL253
A	VAL295

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site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC C 415

Chain	Residue
C	PRO100
C	GLN108
C	ARG112
C	VAL119
C	LEU245
C	GLY248
C	THR252
C	VAL253
C	ASP297
C	ARG299
C	GLN322
C	THR349
C	PHE350
C	GLY351
C	HIS355
C	CYS357
C	GLY359
C	HOH416
C	HOH427
C	HOH468

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Functional Information from PROSITE/UniProt

site_id	PS00086
Number of Residues	10
Details	CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGSHLCLG

Chain	Residue	Details
A	PHE350-GLY359

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: axial binding residue

Chain	Residue	Details
A	LEU358
C	LEU358

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 133

Chain	Residue	Details
A	PRO187	hydrogen bond donor, proton acceptor, proton donor, proton relay
A	THR252	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	VAL253	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	LEU358	electrostatic stabiliser, hydrogen bond acceptor, metal ligand
A	GLY359	electrostatic stabiliser, hydrogen bond donor
A	GLN360	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 133

Chain	Residue	Details
C	PRO187	hydrogen bond donor, proton acceptor, proton donor, proton relay
C	THR252	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	VAL253	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	LEU358	electrostatic stabiliser, hydrogen bond acceptor, metal ligand
C	GLY359	electrostatic stabiliser, hydrogen bond donor
C	GLN360	electrostatic stabiliser, hydrogen bond donor

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