2INP

Structure of the Phenol Hydroxylase-Regulatory Protein Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0004497	molecular_function	monooxygenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
D	0004497	molecular_function	monooxygenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
E	0018662	molecular_function	phenol 2-monooxygenase activity
F	0018662	molecular_function	phenol 2-monooxygenase activity
L	0004497	molecular_function	monooxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 1

Chain	Residue
A	FE3
A	GLU138
A	GLU199
A	GLU233
A	HIS236

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2

Chain	Residue
A	CYS399
A	CYS402
A	CYS432
A	CYS436

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE A 3

Chain	Residue
A	FE1
A	GLU108
A	GLU138
A	HIS141
A	GLU233
A	HOH678
A	HOH750

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE B 4

Chain	Residue
B	FE5
B	GLU108
B	GLU138
B	HIS141
B	HOH501
B	HOH668

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 5

Chain	Residue
B	FE4
B	GLU138
B	GLU199
B	GLU233
B	HIS236

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site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 500

Chain	Residue
B	CYS399
B	CYS402
B	CYS432
B	CYS436

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