1QFJ

CRYSTAL STRUCTURE OF NAD(P)H:FLAVIN OXIDOREDUCTASE FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006826	biological_process	iron ion transport
A	0006979	biological_process	response to oxidative stress
A	0008047	molecular_function	enzyme activator activity
A	0016491	molecular_function	oxidoreductase activity
A	0030091	biological_process	protein repair
A	0042602	molecular_function	riboflavin reductase (NADPH) activity
A	0052875	molecular_function	riboflavin reductase (NAD(P)H) activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006826	biological_process	iron ion transport
B	0006979	biological_process	response to oxidative stress
B	0008047	molecular_function	enzyme activator activity
B	0016491	molecular_function	oxidoreductase activity
B	0030091	biological_process	protein repair
B	0042602	molecular_function	riboflavin reductase (NADPH) activity
B	0052875	molecular_function	riboflavin reductase (NAD(P)H) activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006826	biological_process	iron ion transport
C	0006979	biological_process	response to oxidative stress
C	0008047	molecular_function	enzyme activator activity
C	0016491	molecular_function	oxidoreductase activity
C	0030091	biological_process	protein repair
C	0042602	molecular_function	riboflavin reductase (NADPH) activity
C	0052875	molecular_function	riboflavin reductase (NAD(P)H) activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006826	biological_process	iron ion transport
D	0006979	biological_process	response to oxidative stress
D	0008047	molecular_function	enzyme activator activity
D	0016491	molecular_function	oxidoreductase activity
D	0030091	biological_process	protein repair
D	0042602	molecular_function	riboflavin reductase (NADPH) activity
D	0052875	molecular_function	riboflavin reductase (NAD(P)H) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 601

Chain	Residue
A	TYR35
A	ASP227
A	HOH700
A	HOH701
A	HOH702

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 602

Chain	Residue
B	HOH642
B	PRO47
B	SER49
B	ASP227
B	HOH641

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 603

Chain	Residue
C	TYR35
C	PRO47
C	SER49
C	HOH674
C	HOH676

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 604

Chain	Residue
D	TYR35
D	PRO47
D	ASP227
D	HOH689
D	HOH690
D	HOH691

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY111
B	GLY111
C	GLY111
D	GLY111

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndh

Chain	Residue	Details
A	PHE48

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndh

Chain	Residue	Details
B	PHE48

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndh

Chain	Residue	Details
C	PHE48

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site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ndh

Chain	Residue	Details
D	PHE48

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