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6CXV

Structure of the S167H mutant of human indoleamine 2,3 dioxygenase in complex with tryptophan and cyanide

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
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
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 Residues28
Detailsbinding site for residue HEM A 501
ChainResidue
AHIS167
AARG343
AHIS346
AILE349
AVAL350
ATYR353
AILE354
AGLY378
ATHR379
AGLY380
AGLY381
AVAL170
ATHR382
ALEU384
APHE387
ALEU388
ACYN502
ATRP503
AZCW504
AHOH610
AHOH634
APHE214
AILE217
APHE226
ASER263
AALA264
AGLY265
APHE270

site_idAC2
Number of Residues4
Detailsbinding site for residue CYN A 502
ChainResidue
ASER263
AALA264
AHEM501
ATRP503

site_idAC3
Number of Residues12
Detailsbinding site for residue TRP A 503
ChainResidue
APHE163
AHIS167
APHE226
AARG231
AGLY262
ASER263
AALA264
AILE354
AGLY378
ATHR379
AHEM501
ACYN502

site_idAC4
Number of Residues5
Detailsbinding site for residue ZCW A 504
ChainResidue
APHE270
ALEU342
AARG343
AHIS346
AHEM501

site_idAC5
Number of Residues22
Detailsbinding site for residue HEM B 501
ChainResidue
BHIS167
BPHE214
BPHE226
BSER263
BALA264
BPHE270
BARG343
BHIS346
BILE349
BTYR353
BILE354
BGLY378
BGLY380
BGLY381
BTHR382
BLEU384
BPHE387
BCYN502
BTRP503
BZCW504
BHOH640
BHOH651

site_idAC6
Number of Residues4
Detailsbinding site for residue CYN B 502
ChainResidue
BSER263
BALA264
BHEM501
BTRP503

site_idAC7
Number of Residues13
Detailsbinding site for residue TRP B 503
ChainResidue
BPHE163
BHIS167
BPHE226
BARG231
BLEU234
BGLY262
BSER263
BALA264
BILE354
BGLY378
BTHR379
BHEM501
BCYN502

site_idAC8
Number of Residues5
Detailsbinding site for residue ZCW B 504
ChainResidue
BPHE270
BLEU342
BARG343
BHIS346
BHEM501

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

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PDB entries from 2024-07-24

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