6FPH

The crystal structure of P.fluorescens Kynurenine 3-monooxygenase (KMO) in complex with competitive inhibitor No. 1h

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	36
Details	binding site for residue FAD A 501

Chain	Residue
A	ILE12
A	ALA55
A	ARG110
A	GLY133
A	LEU134
A	ALA164
A	ASP165
A	GLY166
A	ALA170
A	TYR192
A	GLY309
A	GLY13
A	ASP310
A	GLY320
A	GLN321
A	GLY322
A	MET323
A	ASN324
A	CL502
A	E1W503
A	HOH627
A	HOH631
A	GLY15
A	HOH658
A	HOH660
A	HOH667
A	HOH685
A	HOH717
A	HOH759
A	HOH777
A	LEU16
A	ALA17
A	GLU36
A	ARG37
A	ARG38
A	LEU54

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CL A 502

Chain	Residue
A	PRO317
A	GLN321
A	GLY322
A	FAD501

---

site_id	AC3
Number of Residues	12
Details	binding site for residue E1W A 503

Chain	Residue
A	ALA55
A	ARG83
A	TYR97
A	LEU212
A	ILE223
A	PRO317
A	PHE318
A	GLY320
A	ASN368
A	MET372
A	TYR403
A	FAD501

---

site_id	AC4
Number of Residues	34
Details	binding site for residue FAD B 501

Chain	Residue
B	ILE12
B	GLY13
B	GLY15
B	LEU16
B	ALA17
B	GLU36
B	ARG37
B	ARG38
B	LEU54
B	ALA55
B	ARG110
B	GLY133
B	LEU134
B	ALA164
B	ASP165
B	GLY166
B	ALA170
B	GLY309
B	ASP310
B	GLY320
B	GLN321
B	GLY322
B	MET323
B	ASN324
B	CL502
B	E1W503
B	HOH612
B	HOH616
B	HOH636
B	HOH647
B	HOH700
B	HOH712
B	HOH716
B	HOH754

---

site_id	AC5
Number of Residues	4
Details	binding site for residue CL B 502

Chain	Residue
B	PRO317
B	GLN321
B	GLY322
B	FAD501

---

site_id	AC6
Number of Residues	14
Details	binding site for residue E1W B 503

Chain	Residue
B	ASN368
B	MET372
B	TYR403
B	FAD501
B	HOH603
B	ALA55
B	ARG83
B	LEU212
B	ILE214
B	ILE223
B	PHE237
B	PRO317
B	PHE318
B	GLY320

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
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	2
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	2
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	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"},{"source":"PDB","id":"5Y7A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---