6E46

CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) in complex with ferrous heme and tryptophan

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006569	biological_process	L-tryptophan catabolic process
A	0007565	biological_process	female pregnancy
A	0009055	molecular_function	electron transfer activity
A	0019805	biological_process	quinolinate biosynthetic process
A	0020037	molecular_function	heme binding
A	0030485	cellular_component	smooth muscle contractile fiber
A	0032421	cellular_component	stereocilium bundle
A	0033754	molecular_function	indoleamine 2,3-dioxygenase activity
A	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
A	0046006	biological_process	regulation of activated T cell proliferation
A	0046872	molecular_function	metal ion binding
A	0070234	biological_process	positive regulation of T cell apoptotic process
B	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006569	biological_process	L-tryptophan catabolic process
B	0007565	biological_process	female pregnancy
B	0009055	molecular_function	electron transfer activity
B	0019805	biological_process	quinolinate biosynthetic process
B	0020037	molecular_function	heme binding
B	0030485	cellular_component	smooth muscle contractile fiber
B	0032421	cellular_component	stereocilium bundle
B	0033754	molecular_function	indoleamine 2,3-dioxygenase activity
B	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
B	0046006	biological_process	regulation of activated T cell proliferation
B	0046872	molecular_function	metal ion binding
B	0070234	biological_process	positive regulation of T cell apoptotic process
C	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006569	biological_process	L-tryptophan catabolic process
C	0007565	biological_process	female pregnancy
C	0009055	molecular_function	electron transfer activity
C	0019805	biological_process	quinolinate biosynthetic process
C	0020037	molecular_function	heme binding
C	0030485	cellular_component	smooth muscle contractile fiber
C	0032421	cellular_component	stereocilium bundle
C	0033754	molecular_function	indoleamine 2,3-dioxygenase activity
C	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
C	0046006	biological_process	regulation of activated T cell proliferation
C	0046872	molecular_function	metal ion binding
C	0070234	biological_process	positive regulation of T cell apoptotic process
D	0004833	molecular_function	L-tryptophan 2,3-dioxygenase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006569	biological_process	L-tryptophan catabolic process
D	0007565	biological_process	female pregnancy
D	0009055	molecular_function	electron transfer activity
D	0019805	biological_process	quinolinate biosynthetic process
D	0020037	molecular_function	heme binding
D	0030485	cellular_component	smooth muscle contractile fiber
D	0032421	cellular_component	stereocilium bundle
D	0033754	molecular_function	indoleamine 2,3-dioxygenase activity
D	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
D	0046006	biological_process	regulation of activated T cell proliferation
D	0046872	molecular_function	metal ion binding
D	0070234	biological_process	positive regulation of T cell apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue HEM A 501

Chain	Residue
A	TYR126
A	PHE270
A	ARG343
A	HIS346
A	ILE349
A	VAL350
A	TYR353
A	ILE354
A	GLY378
A	GLY380
A	GLY381
A	PHE163
A	THR382
A	PHE387
A	VAL391
A	TRP502
A	HOH612
A	HOH643
A	SER167
A	VAL170
A	PHE214
A	PHE226
A	SER263
A	ALA264
A	GLY265

---

site_id	AC2
Number of Residues	13
Details	binding site for residue TRP A 502

Chain	Residue
A	TYR126
A	PHE163
A	PHE226
A	ARG231
A	LEU234
A	GLY262
A	SER263
A	ALA264
A	ILE354
A	GLY378
A	THR379
A	HEM501
A	HOH605

---

site_id	AC3
Number of Residues	25
Details	binding site for residue HEM B 501

Chain	Residue
B	PHE163
B	SER167
B	VAL170
B	PHE214
B	PHE226
B	SER263
B	ALA264
B	GLY265
B	PHE270
B	PHE291
B	ARG343
B	HIS346
B	ILE349
B	VAL350
B	ILE354
B	GLY378
B	THR379
B	GLY380
B	GLY381
B	THR382
B	VAL391
B	TRP502
B	HOH617
B	HOH671
B	HOH679

---

site_id	AC4
Number of Residues	13
Details	binding site for residue TRP B 502

Chain	Residue
B	TYR126
B	PHE163
B	PHE226
B	ARG231
B	LEU234
B	GLY262
B	SER263
B	ALA264
B	ILE354
B	GLY378
B	THR379
B	HEM501
B	HOH671

---

site_id	AC5
Number of Residues	23
Details	binding site for residue HEM C 501

Chain	Residue
C	TYR126
C	PHE163
C	SER167
C	VAL170
C	PHE214
C	PHE226
C	SER263
C	ALA264
C	GLY265
C	PHE270
C	ARG343
C	HIS346
C	ILE349
C	VAL350
C	ILE354
C	GLY378
C	GLY380
C	GLY381
C	THR382
C	PHE387
C	VAL391
C	TRP503
C	HOH648

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PO4 C 502

Chain	Residue
B	GLU60
B	ARG100
C	PRO33
C	ASP34

---

site_id	AC7
Number of Residues	12
Details	binding site for residue TRP C 503

Chain	Residue
C	TYR126
C	PHE163
C	PHE226
C	ARG231
C	LEU234
C	GLY262
C	SER263
C	ALA264
C	ILE354
C	GLY378
C	THR379
C	HEM501

---

site_id	AC8
Number of Residues	24
Details	binding site for residue HEM D 501

Chain	Residue
D	PHE163
D	SER167
D	VAL170
D	PHE214
D	ILE217
D	PHE226
D	SER263
D	ALA264
D	GLY265
D	PHE270
D	ARG343
D	HIS346
D	ILE349
D	TYR353
D	ILE354
D	GLY378
D	GLY380
D	GLY381
D	THR382
D	VAL391
D	TRP503
D	HOH613
D	HOH623
D	HOH660

---

site_id	AC9
Number of Residues	3
Details	binding site for residue PO4 D 502

Chain	Residue
D	TYR145
D	LYS161
D	HIS220

---

site_id	AD1
Number of Residues	13
Details	binding site for residue TRP D 503

Chain	Residue
D	TYR126
D	PHE163
D	PHE226
D	ARG231
D	LEU234
D	GLY262
D	SER263
D	ALA264
D	ILE354
D	GLY378
D	THR379
D	HEM501
D	HOH623

---

Functional Information from PROSITE/UniProt

site_id	PS00876
Number of Residues	11
Details	IDO_1 Indoleamine 2,3-dioxygenase signature 1. GGSAGQSSvfQ

Chain	Residue	Details
A	GLY261-GLN271

---

site_id	PS00877
Number of Residues	14
Details	IDO_2 Indoleamine 2,3-dioxygenase signature 2. FLQDMrrYMppaHR

Chain	Residue	Details
A	PHE291-ARG304

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"16477023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25313323","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2D0T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PK5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PK6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---