6NBL

Cytochrome P450cam-putidaredoxin complex bound to camphor and cyanide

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
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	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	0046872	molecular_function	metal ion binding
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0009055	molecular_function	electron transfer activity
C	0022900	biological_process	electron transport chain
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	0009055	molecular_function	electron transfer activity
D	0022900	biological_process	electron transport chain
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	17
Details	binding site for residue HEM A 501

Chain	Residue
A	GLN108
A	HIS355
A	LEU356
A	CYS357
A	ALA363
A	CYN502
A	HOH618
A	HOH622
A	HOH642
A	ARG112
A	GLY249
A	THR252
A	VAL253
A	VAL295
A	ARG299
A	THR349
A	PHE350

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CYN A 502

Chain	Residue
A	GLY248
A	THR252
A	HEM501

---

site_id	AC3
Number of Residues	4
Details	binding site for residue CAM A 503

Chain	Residue
A	GLU94
A	GLY248
A	ASP251
A	VAL396

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CA A 504

Chain	Residue
A	GLU198
A	ASP202
B	ALA36
B	HOH636

---

site_id	AC5
Number of Residues	17
Details	binding site for residue HEM B 501

Chain	Residue
B	GLN108
B	PHE111
B	ARG112
B	THR252
B	VAL253
B	LEU294
B	VAL295
B	ARG299
B	THR349
B	PHE350
B	HIS355
B	CYS357
B	ALA363
B	CYN502
B	HOH616
B	HOH617
B	HOH661

---

site_id	AC6
Number of Residues	3
Details	binding site for residue CYN B 502

Chain	Residue
B	GLY248
B	HEM501
B	CAM503

---

site_id	AC7
Number of Residues	4
Details	binding site for residue CAM B 503

Chain	Residue
B	GLU94
B	GLY248
B	ASP251
B	CYN502

---

site_id	AC8
Number of Residues	6
Details	binding site for residue CA B 504

Chain	Residue
A	ALA36
A	HOH619
A	HOH762
B	GLU198
B	ASP202
B	HOH688

---

site_id	AC9
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	AD1
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

---

site_id	AD2
Number of Residues	2
Details	binding site for residue 1N0 B 505

Chain	Residue
B	CYS344
D	CYS19

---

site_id	AD3
Number of Residues	6
Details	binding site for Di-peptide 1N0 C 202 and CYS C 19

Chain	Residue
A	CYS344
C	ALA18
C	GLY20
C	VAL21
C	MET90
C	HOH319

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	208
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8204575","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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
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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