Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5FN0

Crystal structure of Pseudomonas fluorescens kynurenine-3- monooxygenase (KMO) in complex with GSK180

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004497	molecular_function	monooxygenase activity
A	0004502	molecular_function	kynurenine 3-monooxygenase activity
A	0006569	biological_process	L-tryptophan catabolic process
A	0009435	biological_process	NAD+ biosynthetic process
A	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
A	0016491	molecular_function	oxidoreductase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0019674	biological_process	NAD+ metabolic process
A	0019805	biological_process	quinolinate biosynthetic process
A	0043420	biological_process	anthranilate metabolic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0070189	biological_process	kynurenine metabolic process
A	0071949	molecular_function	FAD binding
B	0003824	molecular_function	catalytic activity
B	0004497	molecular_function	monooxygenase activity
B	0004502	molecular_function	kynurenine 3-monooxygenase activity
B	0006569	biological_process	L-tryptophan catabolic process
B	0009435	biological_process	NAD+ biosynthetic process
B	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
B	0016491	molecular_function	oxidoreductase activity
B	0019363	biological_process	pyridine nucleotide biosynthetic process
B	0019674	biological_process	NAD+ metabolic process
B	0019805	biological_process	quinolinate biosynthetic process
B	0043420	biological_process	anthranilate metabolic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0070189	biological_process	kynurenine metabolic process
B	0071949	molecular_function	FAD binding
C	0003824	molecular_function	catalytic activity
C	0004497	molecular_function	monooxygenase activity
C	0004502	molecular_function	kynurenine 3-monooxygenase activity
C	0006569	biological_process	L-tryptophan catabolic process
C	0009435	biological_process	NAD+ biosynthetic process
C	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
C	0016491	molecular_function	oxidoreductase activity
C	0019363	biological_process	pyridine nucleotide biosynthetic process
C	0019674	biological_process	NAD+ metabolic process
C	0019805	biological_process	quinolinate biosynthetic process
C	0043420	biological_process	anthranilate metabolic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0070189	biological_process	kynurenine metabolic process
C	0071949	molecular_function	FAD binding
D	0003824	molecular_function	catalytic activity
D	0004497	molecular_function	monooxygenase activity
D	0004502	molecular_function	kynurenine 3-monooxygenase activity
D	0006569	biological_process	L-tryptophan catabolic process
D	0009435	biological_process	NAD+ biosynthetic process
D	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
D	0016491	molecular_function	oxidoreductase activity
D	0019363	biological_process	pyridine nucleotide biosynthetic process
D	0019674	biological_process	NAD+ metabolic process
D	0019805	biological_process	quinolinate biosynthetic process
D	0043420	biological_process	anthranilate metabolic process
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0070189	biological_process	kynurenine metabolic process
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD A 462

Chain	Residue
A	ILE13
A	ARG39
A	ARG51
A	LEU55
A	ALA56
A	ARG111
A	LEU133
A	GLY134
A	LEU135
A	ALA165
A	ASP166
A	GLY14
A	GLY167
A	ALA171
A	TYR193
A	ASP311
A	PRO318
A	GLY321
A	GLN322
A	GLY323
A	MET324
A	ASN325
A	ALA15
A	HOH2004
A	HOH2012
A	HOH2031
A	JHY4000
A	GLY16
A	LEU17
A	ALA18
A	PHE36
A	GLU37
A	ARG38

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE JHY A 4000

Chain	Residue
A	ALA56
A	ARG84
A	TYR98
A	ILE106
A	PRO318
A	PHE319
A	HIS320
A	GLY321
A	ASN369
A	TYR404
A	FAD462

site_id	AC3
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD B 462

Chain	Residue
B	ILE13
B	GLY14
B	ALA15
B	GLY16
B	LEU17
B	ALA18
B	PHE36
B	GLU37
B	ARG38
B	ARG39
B	ARG51
B	LEU55
B	ALA56
B	ARG111
B	LEU133
B	GLY134
B	LEU135
B	ALA165
B	ASP166
B	GLY167
B	ALA171
B	TYR193
B	ASP311
B	PRO318
B	GLY321
B	GLN322
B	GLY323
B	MET324
B	ASN325
B	HOH2006
B	HOH2014
B	HOH2028
B	HOH2044
B	JHY4000

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE JHY B 4000

Chain	Residue
B	ALA56
B	ARG84
B	TYR98
B	PRO318
B	PHE319
B	HIS320
B	GLY321
B	ASN369
B	MET373
B	TYR404
B	FAD462
B	HOH2047

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD C 462

Chain	Residue
C	ARG51
C	LEU55
C	ALA56
C	ARG111
C	GLY134
C	LEU135
C	ALA165
C	ASP166
C	GLY167
C	ALA171
C	TYR193
C	ASP311
C	PRO318
C	GLY321
C	GLN322
C	GLY323
C	MET324
C	ASN325
C	HOH2010
C	HOH2015
C	HOH2022
C	HOH2027
C	JHY4000
C	ILE13
C	GLY14
C	GLY16
C	LEU17
C	ALA18
C	PHE36
C	GLU37
C	ARG38
C	ARG39

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE JHY C 4000

Chain	Residue
C	ALA56
C	ARG84
C	TYR98
C	ILE106
C	PRO318
C	PHE319
C	HIS320
C	GLY321
C	ASN369
C	MET373
C	TYR404
C	FAD462

site_id	AC7
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD D 462

Chain	Residue
D	ILE13
D	GLY14
D	ALA15
D	GLY16
D	LEU17
D	ALA18
D	PHE36
D	GLU37
D	ARG38
D	ARG39
D	ARG51
D	LEU55
D	ALA56
D	ARG111
D	GLY134
D	LEU135
D	ALA165
D	ASP166
D	GLY167
D	ALA171
D	TYR193
D	ASP311
D	PRO318
D	GLY321
D	GLN322
D	GLY323
D	MET324
D	ASN325
D	HOH2008
D	HOH2013
D	HOH2036
D	HOH2050
D	HOH2051
D	JHY4000

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE JHY D 4000

Chain	Residue
D	ALA56
D	ARG84
D	TYR98
D	ILE106
D	PRO318
D	PHE319
D	HIS320
D	GLY321
D	ASN369
D	TYR404
D	FAD462
D	HOH2054

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28336141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28398044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28604669","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29429898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MZK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5N7T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X6P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X6Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y7A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29208702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y66","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y7A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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