4JWS

Crystal structure of Cytochrome P450cam-putidaredoxin complex

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	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	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006707	biological_process	cholesterol catabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0018683	molecular_function	camphor 5-monooxygenase activity
B	0019383	biological_process	(+)-camphor catabolic process
B	0020037	molecular_function	heme binding
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0140647	biological_process	P450-containing electron transport chain
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0140647	biological_process	P450-containing electron transport chain

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	GLN108
A	GLN322
A	THR349
A	PHE350
A	GLY351
A	HIS355
A	CYS357
A	ALA363
A	HOH602
A	HOH701
A	ARG112
A	LEU245
A	GLY248
A	GLY249
A	THR252
A	VAL295
A	ASP297
A	ARG299

---

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

Chain	Residue
A	GLU198
A	ASP202
B	ALA36

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1N0 A 503

Chain	Residue
A	TYR78
A	SER83
A	PRO105
A	SER354
A	HIS355
C	MET70
C	CYS73

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM B 501

Chain	Residue
B	GLN108
B	ARG112
B	LEU245
B	GLY248
B	GLY249
B	THR252
B	VAL253
B	LEU294
B	ASP297
B	ARG299
B	GLN322
B	THR349
B	PHE350
B	GLY351
B	HIS355
B	CYS357
B	ALA363
B	HOH609
B	HOH644

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 502

Chain	Residue
A	ALA36
A	HOH672
A	HOH673
A	HOH677
B	GLU198
B	ASP202

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1N0 B 503

Chain	Residue
B	TYR78
B	SER83
B	PRO105
B	SER354
B	HIS355
D	MET70
D	CYS73

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES C 201

Chain	Residue
C	GLY37
C	CYS39
C	GLY41
C	ALA43
C	SER44
C	CYS45
C	ALA46
C	CYS48
C	CYS86

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES D 201

Chain	Residue
D	GLY37
D	CYS39
D	GLY41
D	ALA43
D	SER44
D	CYS45
D	ALA46
D	CYS48
D	CYS86

---

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

---

site_id	PS00814
Number of Residues	11
Details	ADX Adrenodoxin family, iron-sulfur binding region signature. CggSaSCATCH

Chain	Residue	Details
C	CYS39-HIS49

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:8204575

Chain	Residue	Details
C	CYS39
C	CYS45
C	CYS48
C	CYS86
D	CYS39
D	CYS45
D	CYS48
D	CYS86

---

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
B	ARG186	hydrogen bond donor, proton acceptor, proton donor, proton relay
B	ASP251	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	THR252	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	CYS357	electrostatic stabiliser, hydrogen bond acceptor, metal ligand
B	LEU358	electrostatic stabiliser, hydrogen bond donor
B	GLY359	electrostatic stabiliser, hydrogen bond donor

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