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5YAK

The crystal structure of human IYD Thr239 mutant with ligand 3-Fluorotyrosine (F-Tyr)

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 Residues22
Detailsbinding site for residue FMN A 501
ChainResidue
AARG100
AARG279
AYOF502
AHOH602
AHOH605
AHOH619
AHOH620
AHOH624
FPRO127
FSER128
FGLY129
AARG101
FHIS131
FTYR212
FSER216
ASER102
AARG104
ALEU176
ATHR178
ATHR237
ATHR238
AALA239

site_idAC2
Number of Residues14
Detailsbinding site for residue YOF A 502
ChainResidue
AGLU157
ATYR161
ATRP169
ALEU173
ATHR178
AASN179
ALYS182
AALA239
AFMN501
AHOH626
FGLY129
FALA130
FTYR212
FHOH627

site_idAC3
Number of Residues23
Detailsbinding site for residue FMN B 501
ChainResidue
BARG100
BARG101
BSER102
BARG104
BLEU176
BTHR178
BVAL236
BTHR237
BTHR238
BALA239
BARG279
BYOF502
BHOH603
BHOH609
BHOH615
BHOH624
CPRO127
CSER128
CGLY129
CHIS131
CTYR212
CSER216
CHOH608

site_idAC4
Number of Residues12
Detailsbinding site for residue YOF B 502
ChainResidue
BGLU157
BTYR161
BLEU173
BLEU176
BLYS182
BALA239
BFMN501
BHOH612
CGLY129
CALA130
CTYR212
CHOH619

site_idAC5
Number of Residues24
Detailsbinding site for residue FMN C 501
ChainResidue
BPRO127
BSER128
BGLY129
BHIS131
BTYR212
BILE215
BSER216
BHOH631
CARG100
CARG101
CSER102
CARG104
CLEU176
CTHR178
CVAL236
CTHR237
CALA239
CLEU277
CARG279
CYOF502
CHOH603
CHOH610
CHOH629
CHOH634

site_idAC6
Number of Residues11
Detailsbinding site for residue YOF C 502
ChainResidue
CTYR161
CLEU173
CTHR178
CLYS182
CALA239
CFMN501
CHOH640
BGLY129
BALA130
BHOH630
CGLU157

site_idAC7
Number of Residues23
Detailsbinding site for residue FMN D 501
ChainResidue
DARG100
DARG101
DSER102
DARG104
DLEU176
DTHR178
DTHR237
DTHR238
DALA239
DARG279
DYOF502
DHOH603
DHOH606
DHOH621
DHOH624
EPRO127
ESER128
EGLY129
EHIS131
ETYR212
EILE215
ESER216
EHOH628

site_idAC8
Number of Residues11
Detailsbinding site for residue YOF D 502
ChainResidue
DGLU157
DTYR161
DLEU173
DLYS182
DALA239
DFMN501
DHOH618
EGLY129
EALA130
ETYR212
EHOH602

site_idAC9
Number of Residues22
Detailsbinding site for residue FMN E 501
ChainResidue
DPRO127
DSER128
DGLY129
DHIS131
DTYR212
DSER216
DHOH619
EARG100
EARG101
ESER102
EARG104
ELEU176
EVAL236
ETHR237
ETHR238
EALA239
EARG279
EYOF502
EHOH609
EHOH611
EHOH621
EHOH626

site_idAD1
Number of Residues10
Detailsbinding site for residue YOF E 502
ChainResidue
DGLY129
DALA130
DHOH631
EGLU157
ETYR161
ELEU173
ELYS182
EALA239
EFMN501
EHOH622

site_idAD2
Number of Residues23
Detailsbinding site for residue FMN F 501
ChainResidue
APRO127
ASER128
AGLY129
AHIS131
ATYR212
AILE215
ASER216
FARG100
FARG101
FSER102
FARG104
FLEU176
FTHR178
FVAL236
FTHR237
FTHR238
FALA239
FARG279
FYOF502
FHOH609
FHOH610
FHOH621
FHOH636

site_idAD3
Number of Residues11
Detailsbinding site for residue YOF F 502
ChainResidue
AGLY129
AALA130
AHOH628
FGLU157
FTYR161
FLEU173
FASN179
FLYS182
FALA239
FFMN501
FHOH605

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
AARG100
DARG100
DTHR237
DARG279
EARG100
ETHR237
EARG279
FARG100
FTHR237
FARG279
ATHR237
AARG279
BARG100
BTHR237
BARG279
CARG100
CTHR237
CARG279

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

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 2024-07-24

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