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4TTC

Crystal structure of homo sapiens IODOTYROSINE DEIODINASE bound to FMN and mono-iodotyrosine (MIT)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0016491molecular_functionoxidoreductase activity
C0016491molecular_functionoxidoreductase activity
D0016491molecular_functionoxidoreductase activity
E0016491molecular_functionoxidoreductase activity
F0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue FMN A 301
ChainResidue
AARG100
AARG279
AIYR302
AHOH425
AHOH426
AHOH427
BPRO127
BSER128
BGLY129
BHIS131
BTYR212
AARG101
BILE215
BSER216
ASER102
AARG104
ALEU176
ATHR178
ATHR237
ATHR238
ATHR239

site_idAC2
Number of Residues10
Detailsbinding site for residue IYR A 302
ChainResidue
AGLU157
ATYR161
ALEU173
ALEU176
ATHR178
AASN179
ALYS182
AFMN301
AHOH437
BALA130

site_idAC3
Number of Residues20
Detailsbinding site for residue FMN B 301
ChainResidue
APRO127
ASER128
AGLY129
ATYR212
ASER216
BARG100
BARG101
BSER102
BARG104
BLEU176
BVAL236
BTHR237
BTHR238
BTHR239
BLEU277
BARG279
BIYR302
BHOH404
BHOH413
BHOH424

site_idAC4
Number of Residues10
Detailsbinding site for residue IYR B 302
ChainResidue
AALA130
BGLU157
BTYR161
BLEU173
BLEU176
BTHR178
BASN179
BLYS182
BFMN301
BHOH435

site_idAC5
Number of Residues21
Detailsbinding site for residue FMN C 301
ChainResidue
CARG100
CARG101
CSER102
CARG104
CLEU176
CTHR178
CVAL236
CTHR237
CTHR238
CTHR239
CARG279
CIYR302
CHOH409
CHOH411
CHOH415
CHOH416
DPRO127
DSER128
DGLY129
DTYR212
DSER216

site_idAC6
Number of Residues10
Detailsbinding site for residue IYR C 302
ChainResidue
CGLU157
CTYR161
CTRP169
CLEU173
CLEU176
CTHR178
CLYS182
CFMN301
DALA130
DTYR211

site_idAC7
Number of Residues19
Detailsbinding site for residue FMN D 301
ChainResidue
DARG101
DSER102
DARG104
DLEU176
DVAL236
DTHR237
DTHR238
DTHR239
DARG279
DIYR302
DHOH410
DHOH416
CPRO127
CSER128
CGLY129
CHIS131
CTYR212
CSER216
DARG100

site_idAC8
Number of Residues10
Detailsbinding site for residue IYR D 302
ChainResidue
CALA130
DGLU157
DTYR161
DLEU173
DLEU176
DASN179
DLYS182
DTHR239
DFMN301
DHOH412

site_idAC9
Number of Residues22
Detailsbinding site for residue FMN E 301
ChainResidue
EARG100
EARG101
ESER102
EARG104
ELEU176
ETHR178
EVAL236
ETHR237
ETHR238
ETHR239
EARG279
EIYR302
EHOH406
EHOH410
EHOH420
FPRO127
FSER128
FGLY129
FHIS131
FTYR212
FSER216
FHOH405

site_idAD1
Number of Residues10
Detailsbinding site for residue IYR E 302
ChainResidue
EGLU157
ETYR161
ELEU173
ELEU176
ETHR178
EASN179
ELYS182
ETHR239
EFMN301
FALA130

site_idAD2
Number of Residues21
Detailsbinding site for residue FMN F 301
ChainResidue
EPRO127
ESER128
EGLY129
ETYR212
EILE215
ESER216
FARG100
FARG101
FSER102
FARG104
FLEU176
FTHR178
FVAL236
FTHR237
FTHR238
FTHR239
FARG279
FIYR302
FHOH404
FHOH406
FHOH409

site_idAD3
Number of Residues9
Detailsbinding site for residue IYR F 302
ChainResidue
EALA130
FGLU157
FTYR161
FLEU173
FLEU176
FTHR178
FASN179
FLYS182
FFMN301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:25395621, ECO:0007744|PDB:4TTB, ECO:0007744|PDB:4TTC
ChainResidueDetails
EARG100
ETHR237
EARG279
FARG100
FTHR237
FARG279
AARG100
ATHR237
AARG279
BARG100
BTHR237
BARG279
CARG100
CTHR237
CARG279
DARG100
DTHR237
DARG279

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:25395621, ECO:0007744|PDB:4TTC
ChainResidueDetails
BTYR161
BLYS182
CSER128
CGLU157
CTYR161
CLYS182
DSER128
DGLU157
DTYR161
DLYS182
ESER128
EGLU157
ETYR161
ELYS182
FSER128
FGLU157
FTYR161
FLYS182
ASER128
AGLU157
ATYR161
ALYS182
BSER128
BGLU157

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4TTC
ChainResidueDetails
AALA130
BALA130
CALA130
DALA130
EALA130
FALA130

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PDB entries from 2024-05-15

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