Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XA3

Crystal Structure of P450BM3 with Benzyloxycarbonyl-L-prolyl-L-phenylalanine

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	24
Details	binding site for residue HEM A 501

Chain	Residue
A	LYS69
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	ALA399
A	CYS400
A	ILE401
A	DMS502
A	PHQ503
A	LEU86
A	HOH604
A	HOH615
A	HOH630
A	HOH637
A	HOH686
A	PHE87
A	TRP96
A	ILE153
A	ALA264
A	THR268
A	THR269
A	THR327

site_id	AC2
Number of Residues	5
Details	binding site for residue DMS A 502

Chain	Residue
A	PHE87
A	ALA264
A	THR268
A	ALA328
A	HEM501

site_id	AC3
Number of Residues	24
Details	binding site for residue HEM B 501

Chain	Residue
B	LYS69
B	LEU86
B	PHE87
B	TRP96
B	ILE153
B	ALA264
B	THR268
B	THR269
B	THR327
B	PHE331
B	PRO392
B	PHE393
B	GLY394
B	ARG398
B	ALA399
B	CYS400
B	ILE401
B	DMS502
B	PHQ503
B	HOH604
B	HOH621
B	HOH628
B	HOH639
B	HOH675

site_id	AC4
Number of Residues	3
Details	binding site for residue DMS B 502

Chain	Residue
B	ALA264
B	THR268
B	HEM501

site_id	AC5
Number of Residues	25
Details	binding site for residue HEM C 501

Chain	Residue
C	LYS69
C	LEU86
C	PHE87
C	TRP96
C	ILE153
C	ALA264
C	THR268
C	THR269
C	THR327
C	PHE331
C	PRO392
C	PHE393
C	GLY394
C	ARG398
C	ALA399
C	CYS400
C	ILE401
C	ALA406
C	DMS502
C	PHQ503
C	HOH626
C	HOH627
C	HOH636
C	HOH658
C	HOH662

site_id	AC6
Number of Residues	4
Details	binding site for residue DMS C 502

Chain	Residue
C	PHE87
C	ALA264
C	THR268
C	HEM501

site_id	AC7
Number of Residues	25
Details	binding site for residue HEM D 501

Chain	Residue
D	ALA399
D	CYS400
D	ILE401
D	GLY402
D	DMS502
D	PHQ503
D	HOH608
D	HOH625
D	HOH633
D	HOH638
D	HOH699
D	LYS69
D	LEU86
D	PHE87
D	TRP96
D	ILE153
D	ALA264
D	THR268
D	THR269
D	THR327
D	PHE331
D	PRO392
D	PHE393
D	GLY394
D	ARG398

site_id	AC8
Number of Residues	4
Details	binding site for residue DMS D 502

Chain	Residue
D	PHE87
D	ALA264
D	THR268
D	HEM501

site_id	AC9
Number of Residues	10
Details	binding site for Di-peptide PRO A 504 and PHQ A 503

Chain	Residue
A	TYR51
A	SER72
A	ALA74
A	LEU75
A	PHE87
A	ALA330
A	MET354
A	LEU437
A	HEM501
A	PHE505

site_id	AD1
Number of Residues	8
Details	binding site for Di-peptide PRO A 504 and PHE A 505

Chain	Residue
A	LEU20
A	TYR51
A	SER72
A	GLN73
A	ALA74
A	MET354
A	PHQ503
A	HOH609

site_id	AD2
Number of Residues	9
Details	binding site for Di-peptide PRO B 504 and PHQ B 503

Chain	Residue
B	TYR51
B	SER72
B	ALA74
B	LEU75
B	PHE87
B	ALA330
B	MET354
B	HEM501
B	PHE505

site_id	AD3
Number of Residues	8
Details	binding site for Di-peptide PRO B 504 and PHE B 505

Chain	Residue
B	LEU20
B	TYR51
B	SER72
B	GLN73
B	ALA74
B	LEU188
B	MET354
B	PHQ503

site_id	AD4
Number of Residues	8
Details	binding site for Di-peptide PRO C 504 and PHE C 505

Chain	Residue
C	LEU20
C	TYR51
C	SER72
C	GLN73
C	ALA74
C	MET354
C	PHQ503
C	HOH637

site_id	AD5
Number of Residues	8
Details	binding site for Di-peptide PRO C 504 and PHQ C 503

Chain	Residue
C	TYR51
C	SER72
C	ALA74
C	PHE87
C	ALA330
C	MET354
C	HEM501
C	PHE505

site_id	AD6
Number of Residues	8
Details	binding site for Di-peptide PRO D 504 and PHE D 505

Chain	Residue
D	LEU20
D	TYR51
D	SER72
D	GLN73
D	ALA74
D	MET354
D	PHQ503
D	HOH616

site_id	AD7
Number of Residues	9
Details	binding site for Di-peptide PRO D 504 and PHQ D 503

Chain	Residue
D	TYR51
D	SER72
D	ALA74
D	LEU75
D	PHE87
D	ALA330
D	MET354
D	HEM501
D	PHE505

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	THR268
B	THR268
C	THR268
D	THR268

Catalytic Information from CSA

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

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