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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SMJ

Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0020037	molecular_function	heme binding
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0020037	molecular_function	heme binding
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 472

Chain	Residue
A	LYS69
A	THR327
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	CYS400
A	ILE401
A	GLY402
A	LEU86
A	PHE87
A	TRP96
A	PHE261
A	GLU264
A	GLY265
A	THR268
A	THR269

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM B 472

Chain	Residue
B	LYS69
B	LEU86
B	PHE87
B	TRP96
B	GLU264
B	GLY265
B	THR268
B	THR327
B	PHE331
B	PHE393
B	GLY394
B	ARG398
B	ALA399
B	CYS400
B	ILE401
B	GLY402

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 472

Chain	Residue
C	LYS69
C	LEU86
C	PHE87
C	TRP96
C	PHE261
C	GLU264
C	GLY265
C	THR268
C	THR269
C	THR327
C	ALA328
C	PHE331
C	PRO392
C	GLY394
C	ARG398
C	ALA399
C	CYS400
C	ILE401
C	GLY402

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM D 472

Chain	Residue
D	LYS69
D	LEU86
D	PHE87
D	TRP96
D	PHE261
D	GLU264
D	GLY265
D	THR268
D	THR269
D	THR327
D	ALA328
D	PHE331
D	PRO392
D	ARG398
D	CYS400
D	ILE401
D	GLY402
D	PHE405

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PAM A 1465

Chain	Residue
A	VAL26
A	TYR51
A	VAL78
A	PHE87

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PAM B 2465

Chain	Residue
B	TYR51

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PAM C 3465

Chain	Residue
C	TYR51
C	PHE87
C	LEU188
C	ILE263
C	GLU264

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PAM D 4465

Chain	Residue
D	LEU20
D	TYR51
D	PHE87
D	LEU188
D	THR260
D	GLU264

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE393-GLY402

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:15020590, ECO:0007744\|PDB:1SMJ

Chain	Residue	Details
A	LEU52
B	LEU52
C	LEU52
D	LEU52

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:10051560, ECO:0000269\|PubMed:11695889, ECO:0000269\|PubMed:11695892, ECO:0000269\|PubMed:14653735, ECO:0000269\|PubMed:15020590, ECO:0000269\|PubMed:15299332, ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:17077084, ECO:0000269\|PubMed:17429965, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18298086, ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:20947800, ECO:0000269\|PubMed:21110374, ECO:0000269\|PubMed:21875028, ECO:0000269\|PubMed:7578081, ECO:0000269\|PubMed:8342039, ECO:0000269\|PubMed:9033595, ECO:0007744\|PDB:1BU7, ECO:0007744\|PDB:1BVY, ECO:0007744\|PDB:1FAG, ECO:0007744\|PDB:1FAH, ECO:0007744\|PDB:1JME, ECO:0007744\|PDB:1JPZ, ECO:0007744\|PDB:1P0V, ECO:0007744\|PDB:1P0W, ECO:0007744\|PDB:1P0X, ECO:0007744\|PDB:1SMI, ECO:0007744\|PDB:1SMJ, ECO:0007744\|PDB:1YQO, ECO:0007744\|PDB:1YQP, ECO:0007744\|PDB:1ZO4, ECO:0007744\|PDB:1ZO9, ECO:0007744\|PDB:1ZOA, ECO:0007744\|PDB:2BMH, ECO:0007744\|PDB:2HPD, ECO:0007744\|PDB:2IJ2, ECO:0007744\|PDB:2IJ3, ECO:0007744\|PDB:2IJ4, ECO:0007744\|PDB:2J1M, ECO:0007744\|PDB:2J4S, ECO:0007744\|PDB:2UWH, ECO:0007744\|PDB:3BEN, ECO:0007744\|PDB:3CBD, ECO:0007744\|PDB:3EKB, ECO:0007744\|PDB:3EKD, ECO:0007744\|PDB:3EKF, ECO:0007744\|PDB:3HF2, ECO:0007744\|PDB:3KX3, ECO:0007744\|PDB:3KX4, ECO:0007744\|PDB:3KX5, ECO:0007744\|PDB:3M4V, ECO:0007744\|PDB:3NPL

Chain	Residue	Details
A	ILE401
B	ILE401
C	ILE401
D	ILE401

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000305\|PubMed:16403573, ECO:0000305\|PubMed:7578081

Chain	Residue	Details
A	THR269
B	THR269
C	THR269
D	THR269

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
A	THR269	electrostatic stabiliser, steric role
A	GLY394	electrostatic stabiliser, steric role
A	ILE401	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
B	THR269	electrostatic stabiliser, steric role
B	GLY394	electrostatic stabiliser, steric role
B	ILE401	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
C	THR269	electrostatic stabiliser, steric role
C	GLY394	electrostatic stabiliser, steric role
C	ILE401	electrostatic stabiliser

site_id	MCSA4
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
D	THR269	electrostatic stabiliser, steric role
D	GLY394	electrostatic stabiliser, steric role
D	ILE401	electrostatic stabiliser

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PDB entries from 2024-04-24

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