5UCW

Cytochrome P411 P-4 A82L A78V F263L amination 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue HEC A 501

Chain	Residue
A	LYS69
A	GLY268
A	THR269
A	THR327
A	VAL328
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	ALA399
A	LEU75
A	SER400
A	ILE401
A	GLY402
A	ALA406
A	HOH610
A	HOH629
A	HOH674
A	HOH700
A	HOH726
A	HOH755
A	LEU86
A	ALA87
A	TRP96
A	PHE107
A	PHE261
A	ALA264
A	GLY265

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site_id	AC2
Number of Residues	26
Details	binding site for residue HEC B 501

Chain	Residue
B	LYS69
B	LEU75
B	LEU86
B	ALA87
B	TRP96
B	PHE261
B	ALA264
B	GLY265
B	GLY268
B	THR269
B	THR327
B	PHE331
B	PRO392
B	PHE393
B	GLY394
B	ARG398
B	ALA399
B	SER400
B	ILE401
B	GLY402
B	HOH610
B	HOH624
B	HOH645
B	HOH657
B	HOH673
B	HOH706

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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

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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	SER400
B	SER400

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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	GLY268
B	GLY268

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
A	GLY268	electrostatic stabiliser, steric role
A	PHE393	electrostatic stabiliser, steric role
A	SER400	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
B	GLY268	electrostatic stabiliser, steric role
B	PHE393	electrostatic stabiliser, steric role
B	SER400	electrostatic stabiliser

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