4HGI

Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset II)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	LYS69
A	THR327
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	ALA399
A	CYS400
A	ILE401
A	GLY402
A	LEU86
A	SYN502
A	HOH603
A	HOH604
A	HOH605
A	HOH606
A	HOH639
A	HOH782
A	HOH1056
A	ALA87
A	TRP96
A	PHE107
A	ALA264
A	GLY265
A	THR268
A	THR269

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SYN A 502

Chain	Residue
A	LEU75
A	ALA87
A	ILE263
A	ALA264
A	THR268
A	ALA328
A	LEU437
A	HEM501
A	HOH782
A	HOH1043
A	HOH1056

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	ASP68
A	THR91
A	HIS92
A	TYR334
A	LYS336
A	HOH654

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	GLN128
A	GLU131
A	ARG132
A	HOH1051
A	HOH1077
B	ASP121
B	ARG161

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG A 505

Chain	Residue
A	TYR334
A	ALA335
A	LYS349
A	GLY350
A	HOH769
A	HOH1023

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 506

Chain	Residue
A	HIS100
A	GLY396
A	GLN397
A	ALA399
A	ILE401
A	HOH639
A	HOH1022

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 501

Chain	Residue
A	ASP121
A	ARG161
B	GLN128
B	ARG132
B	HOH991

---

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEM B 502

Chain	Residue
B	LYS69
B	LEU86
B	ALA87
B	TRP96
B	PHE107
B	ILE153
B	ALA264
B	GLY265
B	THR268
B	THR269
B	THR327
B	PHE331
B	PRO392
B	PHE393
B	GLY394
B	ARG398
B	ALA399
B	CYS400
B	ILE401
B	GLY402
B	SYN503
B	HOH604
B	HOH613
B	HOH630
B	HOH640
B	HOH659
B	HOH993
B	HOH1005

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SYN B 503

Chain	Residue
B	ALA264
B	THR268
B	ALA328
B	LEU437
B	HEM502
B	HOH993
B	HOH1005
B	LEU75
B	ALA87

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 504

Chain	Residue
B	ASP68
B	THR91
B	LYS336
B	HOH724
B	HOH932

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MES B 505

Chain	Residue
B	ILE366
B	TRP367
B	ARG375
B	ILE385
B	PRO386
B	HOH684

---

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	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ

Chain	Residue	Details
A	TYR51
B	TYR51

---

site_id	SWS_FT_FI2
Number of Residues	2
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

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081

Chain	Residue	Details
A	THR268
B	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

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