Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2UWH

Cytochrome P450 BM3 mutant in complex with palmitic acid

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
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0020037	molecular_function	heme binding
F	0004497	molecular_function	monooxygenase activity
F	0005506	molecular_function	iron ion binding
F	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A1459

Chain	Residue
A	LYS69
A	THR269
A	THR327
A	ALA328
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	CYS400
A	ILE401
A	LEU86
A	ALA406
A	HOH2011
A	HOH2063
A	HOH2064
A	HOH2087
A	HOH2088
A	PHE87
A	TRP96
A	PHE107
A	PHE261
A	ALA264
A	GLY265
A	THR268

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM A1460

Chain	Residue
A	TYR51
A	PHE87
A	LEU188
A	ALA330
A	HOH2089

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B1459

Chain	Residue
B	LYS69
B	LEU86
B	PHE87
B	TRP96
B	PHE107
B	PHE261
B	ALA264
B	GLY265
B	THR268
B	THR269
B	THR327
B	PHE331
B	PRO392
B	PHE393
B	GLY394
B	ARG398
B	CYS400
B	ILE401
B	HOH2072
B	HOH2084
B	HOH2093
B	HOH2094

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PLM B1460

Chain	Residue
B	ARG47
B	TYR51
B	PHE87

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM C1459

Chain	Residue
C	LYS69
C	LEU86
C	PHE87
C	TRP96
C	PHE107
C	PHE261
C	ALA264
C	GLY265
C	THR268
C	THR269
C	LEU272
C	THR327
C	ALA328
C	PHE331
C	PRO392
C	PHE393
C	ARG398
C	CYS400
C	ILE401
C	GLY402
C	ALA406
C	HOH2086
C	HOH2087
C	HOH2088
C	HOH2089

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM C1460

Chain	Residue
C	LEU20
C	ARG47
C	TYR51
C	LEU188
C	LEU437

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D1459

Chain	Residue
D	PHE393
D	GLY394
D	ARG398
D	CYS400
D	ILE401
D	ALA406
D	HOH2082
D	HOH2083
D	LYS69
D	LEU86
D	PHE87
D	TRP96
D	PHE107
D	PHE261
D	ALA264
D	GLY265
D	THR268
D	THR269
D	THR327
D	ALA328
D	PHE331
D	PRO392

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PLM D1460

Chain	Residue
D	LEU20
D	ARG47
D	TYR51
D	PHE87
D	LEU188
D	ALA264
D	PRO329

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM E1459

Chain	Residue
E	LYS69
E	LEU86
E	PHE87
E	TRP96
E	PHE107
E	PHE261
E	ALA264
E	GLY265
E	THR268
E	THR269
E	LEU272
E	THR327
E	ALA328
E	PHE331
E	PRO392
E	PHE393
E	ARG398
E	CYS400
E	ALA406
E	HOH2083

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PLM E1460

Chain	Residue
E	PHE42
E	ARG47
E	TYR51
E	PHE87

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM F1459

Chain	Residue
F	LYS69
F	LEU86
F	PHE87
F	TRP96
F	PHE107
F	PHE261
F	ALA264
F	GLY265
F	THR268
F	THR269
F	THR327
F	ALA328
F	PHE331
F	PRO392
F	PHE393
F	ARG398
F	CYS400
F	ILE401
F	GLY402
F	ALA406
F	HOH2056
F	HOH2070
F	HOH2082

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM F1460

Chain	Residue
F	VAL26
F	TYR51
F	ALA264
F	ALA330
F	LEU437

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	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15020590, ECO:0007744\|PDB:1SMJ

Chain	Residue	Details
A	LEU52
B	LEU52
C	LEU52
D	LEU52
E	LEU52
F	LEU52

site_id	SWS_FT_FI2
Number of Residues	6
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
E	ILE401
F	ILE401

site_id	SWS_FT_FI3
Number of Residues	6
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
E	THR269
F	THR269

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
A	THR268
A	GLU267

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
B	THR268
B	GLU267

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
C	THR268
C	GLU267

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
D	THR268
D	GLU267

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
E	THR268
E	GLU267

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
F	THR268
F	GLU267

site_id	MCSA1
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
A	THR268	electrostatic stabiliser, steric role
A	PHE393	electrostatic stabiliser, steric role
A	CYS400	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
B	THR268	electrostatic stabiliser, steric role
B	PHE393	electrostatic stabiliser, steric role
B	CYS400	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
C	THR268	electrostatic stabiliser, steric role
C	PHE393	electrostatic stabiliser, steric role
C	CYS400	electrostatic stabiliser

site_id	MCSA4
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
D	THR268	electrostatic stabiliser, steric role
D	PHE393	electrostatic stabiliser, steric role
D	CYS400	electrostatic stabiliser

site_id	MCSA5
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
E	THR268	electrostatic stabiliser, steric role
E	PHE393	electrostatic stabiliser, steric role
E	CYS400	electrostatic stabiliser

site_id	MCSA6
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
F	THR268	electrostatic stabiliser, steric role
F	PHE393	electrostatic stabiliser, steric role
F	CYS400	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)