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6VBN

Crystal Structure of hTDO2 bound to inhibitor GNE1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004833molecular_functiontryptophan 2,3-dioxygenase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006568biological_processtryptophan metabolic process
A0006569biological_processtryptophan catabolic process
A0016491molecular_functionoxidoreductase activity
A0016597molecular_functionamino acid binding
A0019441biological_processtryptophan catabolic process to kynurenine
A0019442biological_processtryptophan catabolic process to acetyl-CoA
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051289biological_processprotein homotetramerization
A1904842biological_processresponse to nitroglycerin
B0004833molecular_functiontryptophan 2,3-dioxygenase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006568biological_processtryptophan metabolic process
B0006569biological_processtryptophan catabolic process
B0016491molecular_functionoxidoreductase activity
B0016597molecular_functionamino acid binding
B0019441biological_processtryptophan catabolic process to kynurenine
B0019442biological_processtryptophan catabolic process to acetyl-CoA
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0051289biological_processprotein homotetramerization
B1904842biological_processresponse to nitroglycerin
C0004833molecular_functiontryptophan 2,3-dioxygenase activity
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006568biological_processtryptophan metabolic process
C0006569biological_processtryptophan catabolic process
C0016491molecular_functionoxidoreductase activity
C0016597molecular_functionamino acid binding
C0019441biological_processtryptophan catabolic process to kynurenine
C0019442biological_processtryptophan catabolic process to acetyl-CoA
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0051289biological_processprotein homotetramerization
C1904842biological_processresponse to nitroglycerin
D0004833molecular_functiontryptophan 2,3-dioxygenase activity
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0006568biological_processtryptophan metabolic process
D0006569biological_processtryptophan catabolic process
D0016491molecular_functionoxidoreductase activity
D0016597molecular_functionamino acid binding
D0019441biological_processtryptophan catabolic process to kynurenine
D0019442biological_processtryptophan catabolic process to acetyl-CoA
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0051289biological_processprotein homotetramerization
D1904842biological_processresponse to nitroglycerin
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue HEM A 401
ChainResidue
APHE72
AARG159
ATRP324
AHIS328
AVAL332
AMET335
ATHR342
ATYR350
ALEU351
AQVY402
BTYR42
AHIS76
ATYR79
ALEU132
APHE140
ASER151
AGLY152
APHE153
APHE158

site_idAC2
Number of Residues9
Detailsbinding site for residue QVY A 402
ChainResidue
APHE72
AHIS76
APHE140
AALA150
AGLY152
ALEU336
AHEM401
BTYR42
BTYR45

site_idAC3
Number of Residues19
Detailsbinding site for residue HEM B 401
ChainResidue
ATYR42
BPHE72
BHIS76
BTYR79
BLEU132
BSER151
BGLY152
BPHE153
BPHE158
BARG159
BTRP324
BHIS328
BMET331
BVAL332
BLEU336
BTHR342
BTYR350
BLEU351
BQVY402

site_idAC4
Number of Residues8
Detailsbinding site for residue QVY B 402
ChainResidue
ATYR42
ATYR45
BPHE72
BHIS76
BPHE140
BALA150
BGLY152
BHEM401

site_idAC5
Number of Residues19
Detailsbinding site for residue HEM C 401
ChainResidue
CPHE72
CHIS76
CTYR79
CLEU132
CPHE140
CSER151
CGLY152
CPHE153
CPHE158
CARG159
CTRP324
CHIS328
CVAL332
CLEU336
CTHR342
CTYR350
CLEU351
CQVY403
DTYR42

site_idAC6
Number of Residues9
Detailsbinding site for residue QVY C 402
ChainResidue
CTYR42
CTYR45
DHIS76
DPHE140
DLEU147
DALA150
DGLY152
DLEU336
DHEM401

site_idAC7
Number of Residues10
Detailsbinding site for residue QVY C 403
ChainResidue
CPHE72
CHIS76
CPHE140
CLEU147
CALA150
CGLY152
CLEU336
CHEM401
DTYR42
DTYR45

site_idAC8
Number of Residues20
Detailsbinding site for residue HEM D 401
ChainResidue
DSER151
DGLY152
DPHE153
DPHE158
DARG159
DTRP324
DHIS328
DMET331
DVAL332
DMET335
DLEU336
DTHR342
DTYR350
DLEU351
CTYR42
CQVY402
DPHE72
DHIS76
DTYR79
DLEU132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9
ChainResidueDetails
APHE72
DPHE72
DARG144
DTHR342
AARG144
ATHR342
BPHE72
BARG144
BTHR342
CPHE72
CARG144
CTHR342

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_03020, ECO:0000269|PubMed:27762317, ECO:0007744|PDB:5TI9
ChainResidueDetails
AHIS328
BHIS328
CHIS328
DHIS328

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PDB entries from 2024-04-24

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