3WRJ

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	0016491	molecular_function	oxidoreductase 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	0046872	molecular_function	metal ion binding
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0018683	molecular_function	camphor 5-monooxygenase activity
E	0019383	biological_process	(+)-camphor catabolic process
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	PRO100
A	ASP297
A	ARG299
A	GLN322
A	THR349
A	PHE350
A	GLY351
A	HIS355
A	CYS357
A	GLY359
A	CAM503
A	THR101
A	HOH736
A	GLN108
A	ARG112
A	LEU245
A	GLY248
A	GLY249
A	THR252
A	VAL253

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 502

Chain	Residue
A	GLU84
A	GLY93
A	GLU94
A	TYR96
A	HOH754

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAM A 503

Chain	Residue
A	PHE87
A	TYR96
A	LEU244
A	VAL295
A	HEM501

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM E 501

Chain	Residue
E	PRO100
E	THR101
E	GLN108
E	ARG112
E	LEU245
E	GLY248
E	GLY249
E	THR252
E	VAL253
E	LEU294
E	ASP297
E	ARG299
E	GLN322
E	THR349
E	PHE350
E	GLY351
E	HIS355
E	CYS357
E	GLY359
E	CAM503
E	HOH642

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K E 502

Chain	Residue
E	GLU84
E	GLY93
E	GLU94
E	TYR96

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAM E 503

Chain	Residue
E	PHE87
E	TYR96
E	LEU244
E	VAL295
E	HEM501

---

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 site: {"description":"axial binding residue"}

Chain

Residue

Details

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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

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 133

Chain

Residue

Details

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