3WRK

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	ARG112
A	GLN322
A	THR349
A	PHE350
A	GLY351
A	HIS355
A	CYS357
A	GLY359
A	CAM502
A	HOH623
A	HOH655
A	LEU244
A	LEU245
A	GLY248
A	GLY249
A	THR252
A	LEU294
A	ASP297
A	ARG299

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CAM A 502

Chain	Residue
A	PHE87
A	GLY248
A	HEM501

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site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM D 501

Chain	Residue
D	ARG112
D	LEU244
D	LEU245
D	GLY248
D	GLY249
D	THR252
D	ASP297
D	ARG299
D	GLN322
D	THR349
D	PHE350
D	GLY351
D	HIS355
D	CYS357
D	GLY359
D	CAM502
D	HOH616
D	HOH632

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CAM D 502

Chain	Residue
D	PHE87
D	GLY248
D	HEM501

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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	CYS357
D	CYS357

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 133

Chain	Residue	Details
A	ARG186	hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ASP251	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	THR252	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	CYS357	electrostatic stabiliser, hydrogen bond acceptor, metal ligand
A	LEU358	electrostatic stabiliser, hydrogen bond donor
A	GLY359	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 133

Chain	Residue	Details
D	ARG186	hydrogen bond donor, proton acceptor, proton donor, proton relay
D	ASP251	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	THR252	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	CYS357	electrostatic stabiliser, hydrogen bond acceptor, metal ligand
D	LEU358	electrostatic stabiliser, hydrogen bond donor
D	GLY359	electrostatic stabiliser, hydrogen bond donor

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