Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PYY

Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PF-06840003 in Active Site and Exo site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006568	biological_process	L-tryptophan metabolic process
A	0006569	biological_process	L-tryptophan catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016597	molecular_function	amino acid binding
A	0019441	biological_process	L-tryptophan catabolic process to kynurenine
A	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0042802	molecular_function	identical protein binding
A	0045471	biological_process	response to ethanol
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051289	biological_process	protein homotetramerization
A	0051414	biological_process	response to cortisol
A	1904842	biological_process	response to nitroglycerin
B	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006568	biological_process	L-tryptophan metabolic process
B	0006569	biological_process	L-tryptophan catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016597	molecular_function	amino acid binding
B	0019441	biological_process	L-tryptophan catabolic process to kynurenine
B	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0042802	molecular_function	identical protein binding
B	0045471	biological_process	response to ethanol
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	0051289	biological_process	protein homotetramerization
B	0051414	biological_process	response to cortisol
B	1904842	biological_process	response to nitroglycerin
C	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006568	biological_process	L-tryptophan metabolic process
C	0006569	biological_process	L-tryptophan catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016597	molecular_function	amino acid binding
C	0019441	biological_process	L-tryptophan catabolic process to kynurenine
C	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0042802	molecular_function	identical protein binding
C	0045471	biological_process	response to ethanol
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051289	biological_process	protein homotetramerization
C	0051414	biological_process	response to cortisol
C	1904842	biological_process	response to nitroglycerin
D	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006568	biological_process	L-tryptophan metabolic process
D	0006569	biological_process	L-tryptophan catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016597	molecular_function	amino acid binding
D	0019441	biological_process	L-tryptophan catabolic process to kynurenine
D	0019442	biological_process	L-tryptophan catabolic process to acetyl-CoA
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0042802	molecular_function	identical protein binding
D	0045471	biological_process	response to ethanol
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0051289	biological_process	protein homotetramerization
D	0051414	biological_process	response to cortisol
D	1904842	biological_process	response to nitroglycerin

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue HEM A 401

Chain	Residue
A	HIS76
A	ARG325
A	HIS328
A	MET331
A	VAL332
A	MET335
A	GLY341
A	GLY343
A	SER345
A	TYR350
A	H7S402
A	TYR79
A	HOH502
A	HOH552
A	PHE140
A	SER151
A	GLY152
A	PHE153
A	PHE158
A	ARG159
A	ASN176

site_id	AC2
Number of Residues	10
Details	binding site for residue H7S A 402

Chain	Residue
A	PHE72
A	HIS76
A	ARG144
A	ALA150
A	SER151
A	LEU336
A	THR342
A	HEM401
B	TYR42
B	TYR45

site_id	AC3
Number of Residues	9
Details	binding site for residue H7S A 403

Chain	Residue
A	ARG103
A	GLU105
A	TRP208
A	ARG211
A	THR212
A	PRO213
A	ARG303
A	PHE304
A	HOH533

site_id	AC4
Number of Residues	22
Details	binding site for residue HEM B 401

Chain	Residue
B	HIS76
B	TYR79
B	LEU132
B	SER151
B	GLY152
B	PHE153
B	PHE158
B	ARG159
B	ARG325
B	HIS328
B	MET331
B	VAL332
B	GLY341
B	THR342
B	GLY343
B	GLY344
B	SER345
B	GLY347
B	TYR350
B	H7S402
B	HOH503
B	HOH538

site_id	AC5
Number of Residues	10
Details	binding site for residue H7S B 402

Chain	Residue
A	TYR42
A	TYR45
B	PHE72
B	HIS76
B	ARG144
B	ALA150
B	SER151
B	LEU336
B	THR342
B	HEM401

site_id	AC6
Number of Residues	11
Details	binding site for residue H7S B 403

Chain	Residue
B	VAL102
B	ARG103
B	GLU105
B	TRP208
B	ARG211
B	THR212
B	PRO213
B	ARG303
B	PHE304
B	HOH517
B	HOH532

site_id	AC7
Number of Residues	21
Details	binding site for residue HEM C 401

Chain	Residue
C	TYR350
C	THR354
C	H7S402
C	HOH501
D	TYR42
C	HIS76
C	MET135
C	SER151
C	GLY152
C	PHE153
C	PHE158
C	ARG159
C	TRP324
C	HIS328
C	MET331
C	VAL332
C	MET335
C	GLY341
C	GLY343
C	SER345
C	GLY347

site_id	AC8
Number of Residues	10
Details	binding site for residue H7S C 402

Chain	Residue
C	PHE72
C	HIS76
C	ARG144
C	ALA150
C	SER151
C	LEU336
C	THR342
C	HEM401
D	TYR42
D	TYR45

site_id	AC9
Number of Residues	8
Details	binding site for residue H7S C 403

Chain	Residue
C	ARG103
C	GLU105
C	TRP208
C	ARG211
C	THR212
C	PRO213
C	ARG303
C	PHE304

site_id	AD1
Number of Residues	19
Details	binding site for residue HEM D 401

Chain	Residue
C	TYR42
D	PHE72
D	HIS76
D	TYR79
D	SER151
D	GLY152
D	PHE158
D	ARG159
D	TYR175
D	ARG325
D	HIS328
D	MET331
D	VAL332
D	MET335
D	TYR350
D	THR354
D	H7S402
D	HOH534
D	HOH550

site_id	AD2
Number of Residues	7
Details	binding site for residue H7S D 402

Chain	Residue
C	TYR42
C	TYR45
D	PHE72
D	HIS76
D	ALA150
D	SER151
D	HEM401

site_id	AD3
Number of Residues	7
Details	binding site for residue H7S D 403

Chain	Residue
D	ARG103
D	TRP208
D	ARG211
D	THR212
D	PRO213
D	ARG303
D	PHE304

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	23
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_03020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27762317","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TI9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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