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4U72

Crystal structure of 4-phenylimidazole bound form of human indoleamine 2,3-dioxygenase (A260G mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002376biological_processimmune system process
A0002666biological_processpositive regulation of T cell tolerance induction
A0002678biological_processpositive regulation of chronic inflammatory response
A0002830biological_processpositive regulation of type 2 immune response
A0004833molecular_functiontryptophan 2,3-dioxygenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006569biological_processtryptophan catabolic process
A0006954biological_processinflammatory response
A0007565biological_processfemale pregnancy
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0019441biological_processtryptophan catabolic process to kynurenine
A0020037molecular_functionheme binding
A0030485cellular_componentsmooth muscle contractile fiber
A0032421cellular_componentstereocilium bundle
A0032496biological_processresponse to lipopolysaccharide
A0032693biological_processnegative regulation of interleukin-10 production
A0032735biological_processpositive regulation of interleukin-12 production
A0033555biological_processmulticellular organismal response to stress
A0033754molecular_functionindoleamine 2,3-dioxygenase activity
A0034276biological_processkynurenic acid biosynthetic process
A0034354biological_process'de novo' NAD biosynthetic process from tryptophan
A0036269biological_processswimming behavior
A0042098biological_processT cell proliferation
A0042130biological_processnegative regulation of T cell proliferation
A0043065biological_processpositive regulation of apoptotic process
A0046006biological_processregulation of activated T cell proliferation
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0070233biological_processnegative regulation of T cell apoptotic process
A0070234biological_processpositive regulation of T cell apoptotic process
B0002376biological_processimmune system process
B0002666biological_processpositive regulation of T cell tolerance induction
B0002678biological_processpositive regulation of chronic inflammatory response
B0002830biological_processpositive regulation of type 2 immune response
B0004833molecular_functiontryptophan 2,3-dioxygenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006569biological_processtryptophan catabolic process
B0006954biological_processinflammatory response
B0007565biological_processfemale pregnancy
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0019441biological_processtryptophan catabolic process to kynurenine
B0020037molecular_functionheme binding
B0030485cellular_componentsmooth muscle contractile fiber
B0032421cellular_componentstereocilium bundle
B0032496biological_processresponse to lipopolysaccharide
B0032693biological_processnegative regulation of interleukin-10 production
B0032735biological_processpositive regulation of interleukin-12 production
B0033555biological_processmulticellular organismal response to stress
B0033754molecular_functionindoleamine 2,3-dioxygenase activity
B0034276biological_processkynurenic acid biosynthetic process
B0034354biological_process'de novo' NAD biosynthetic process from tryptophan
B0036269biological_processswimming behavior
B0042098biological_processT cell proliferation
B0042130biological_processnegative regulation of T cell proliferation
B0043065biological_processpositive regulation of apoptotic process
B0046006biological_processregulation of activated T cell proliferation
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0070233biological_processnegative regulation of T cell apoptotic process
B0070234biological_processpositive regulation of T cell apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 501
ChainResidue
ATYR126
AHIS346
AILE349
AVAL350
ATYR353
ALEU384
ALEU388
AVAL391
APIM502
ANHE503
ANHE504
APHE163
AHOH619
AHOH629
AHOH672
ASER167
APHE214
APHE226
ASER263
AALA264
APHE270
AARG343

site_idAC2
Number of Residues7
Detailsbinding site for residue PIM A 502
ChainResidue
AVAL130
APHE163
ASER167
ASER263
AALA264
AHEM501
ANHE503

site_idAC3
Number of Residues11
Detailsbinding site for residue NHE A 503
ChainResidue
APHE163
APHE226
ASER235
AGLY236
AGLY260
AGLY261
AGLY262
AHEM501
APIM502
ANHE504
AHOH684

site_idAC4
Number of Residues7
Detailsbinding site for residue NHE A 504
ChainResidue
AARG231
ALYS238
AGLY260
AHIS287
APHE291
AHEM501
ANHE503

site_idAC5
Number of Residues22
Detailsbinding site for residue HEM B 501
ChainResidue
BPHE163
BSER167
BPHE214
BPHE226
BSER263
BALA264
BPHE270
BARG343
BHIS346
BILE349
BVAL350
BTYR353
BILE354
BLEU384
BLEU388
BVAL391
BPIM502
BNHE503
BNHE504
BHOH632
BHOH635
BHOH686

site_idAC6
Number of Residues7
Detailsbinding site for residue PIM B 502
ChainResidue
BVAL130
BPHE163
BSER167
BSER263
BALA264
BHEM501
BNHE503

site_idAC7
Number of Residues11
Detailsbinding site for residue NHE B 503
ChainResidue
BPHE163
BPHE226
BSER235
BGLY236
BGLY260
BGLY261
BGLY262
BHEM501
BPIM502
BNHE504
BHOH671

site_idAC8
Number of Residues10
Detailsbinding site for residue NHE B 504
ChainResidue
BARG231
BLYS238
BGLY260
BHIS287
BPHE291
BLEU384
BPHE387
BHEM501
BNHE503
BHOH652

Functional Information from PROSITE/UniProt
site_idPS00876
Number of Residues11
DetailsIDO_1 Indoleamine 2,3-dioxygenase signature 1. GGSAGQSSvfQ
ChainResidueDetails
AGLY261-GLN271

site_idPS00877
Number of Residues14
DetailsIDO_2 Indoleamine 2,3-dioxygenase signature 2. FLQDMrrYMppaHR
ChainResidueDetails
APHE291-ARG304

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:16477023, ECO:0000269|PubMed:25313323, ECO:0007744|PDB:2D0T, ECO:0007744|PDB:2D0U, ECO:0007744|PDB:4PK5, ECO:0007744|PDB:4PK6
ChainResidueDetails
AHIS346
BHIS346

218853

PDB entries from 2024-04-24

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