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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H24

Cytochrome P450BM3-CIS cyclopropanation catalyst

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	23
Details	BINDING SITE FOR RESIDUE HEM A 500

Chain	Residue
A	LYS69
A	THR327
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	ALA399
A	CYS400
A	ILE401
A	ALA406
A	LEU86
A	HOH604
A	HOH607
A	HOH626
A	HOH649
A	VAL87
A	TRP96
A	ILE153
A	ALA264
A	GLY265
A	ALA268
A	THR269

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 500

Chain	Residue
B	LYS69
B	LEU86
B	VAL87
B	TRP96
B	PHE107
B	PHE261
B	GLY265
B	ALA268
B	THR269
B	PHE331
B	PRO392
B	PHE393
B	GLY394
B	ARG398
B	CYS400
B	ILE401
B	GLY402
B	ALA406
B	HOH605
B	HOH618
B	HOH624

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM C 500

Chain	Residue
C	LYS69
C	LEU75
C	LEU86
C	VAL87
C	TRP96
C	PHE261
C	ALA264
C	GLY265
C	ALA268
C	THR269
C	THR327
C	ALA328
C	PHE331
C	PRO392
C	PHE393
C	GLY394
C	ARG398
C	ALA399
C	CYS400
C	ILE401
C	PHE405
C	HOH610
C	HOH624
C	HOH631

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM D 500

Chain	Residue
D	LYS69
D	LEU86
D	VAL87
D	TRP96
D	PHE107
D	PHE261
D	ALA264
D	GLY265
D	ALA268
D	THR269
D	THR327
D	PHE331
D	PRO392
D	PHE393
D	GLY394
D	ARG398
D	CYS400
D	ILE401
D	GLY402
D	HOH601
D	HOH602
D	HOH615
D	HOH619
D	HOH633

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	TYR51
B	TYR51
C	TYR51
D	TYR51

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	CYS400
B	CYS400
C	CYS400
D	CYS400

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	ALA268
B	ALA268
C	ALA268
D	ALA268

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
A	ALA268	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	ALA268	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	ALA268	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	ALA268	electrostatic stabiliser, steric role
D	PHE393	electrostatic stabiliser, steric role
D	CYS400	electrostatic stabiliser

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PDB entries from 2024-07-31

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