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6TYK

Crystal structure of iodotyrosine deiodinase (IYD) in the semiquinone form bound to FMN and 3-iodo-L-tyrosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0006570biological_processtyrosine metabolic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0042403biological_processthyroid hormone metabolic process
A0072545molecular_functionL-tyrosine binding
A0140616molecular_functioniodotyrosine deiodinase activity
B0006570biological_processtyrosine metabolic process
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0042403biological_processthyroid hormone metabolic process
B0072545molecular_functionL-tyrosine binding
B0140616molecular_functioniodotyrosine deiodinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue FMN A 301
ChainResidue
ALYS12
ALYS173
ATYR174
AARG176
AIYR302
ACL303
AHOH425
AHOH436
AHOH437
AHOH440
BPRO38
ATHR13
BSER39
BGLY40
BTYR112
BSER116
AARG15
ATRP82
APHE88
AVAL136
APRO137
ATYR138
ATHR139

site_idAC2
Number of Residues11
Detailsbinding site for residue IYR A 302
ChainResidue
AGLU68
ATYR72
ATRP82
ALEU83
ALYS92
ATYR138
ATHR139
AFMN301
AHOH493
BGLY40
BMET41

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 303
ChainResidue
AARG11
ATHR13
APRO137
AFMN301
BPRO38

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
AARG157
AHOH457

site_idAC5
Number of Residues5
Detailsbinding site for residue CL A 305
ChainResidue
AARG15
AARG16
APRO170
ALYS171
AHOH584

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
ATRP82
ALYS86
BASN42
BASN177

site_idAC7
Number of Residues4
Detailsbinding site for residue CL A 307
ChainResidue
AGLU54
AGLY58
AHOH469
AHOH477

site_idAC8
Number of Residues23
Detailsbinding site for residue FMN B 301
ChainResidue
APRO38
ASER39
AGLY40
ATYR112
ASER116
BLYS12
BTHR13
BARG15
BTRP82
BPHE88
BVAL136
BPRO137
BTYR138
BTHR139
BLYS173
BTYR174
BARG176
BIYR302
BCL303
BHOH422
BHOH426
BHOH440
BHOH470

site_idAC9
Number of Residues11
Detailsbinding site for residue IYR B 302
ChainResidue
AGLY40
AMET41
BGLU68
BTYR72
BLEU83
BLYS92
BTYR138
BTHR139
BFMN301
BHOH460
BHOH471

site_idAD1
Number of Residues5
Detailsbinding site for residue CL B 303
ChainResidue
APRO38
BARG11
BTHR13
BPRO137
BFMN301

site_idAD2
Number of Residues4
Detailsbinding site for residue CL B 304
ChainResidue
AASN42
AASN177
BTRP82
BLYS86

site_idAD3
Number of Residues8
Detailsbinding site for residue IYR B 305
ChainResidue
AHOH497
BGLU73
BASN74
BARG114
BGLU115
BHOH430
AARG114
AGLU115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0007744|PDB:6PZ0, ECO:0007744|PDB:6Q1B, ECO:0007744|PDB:6Q1L, ECO:0007744|PDB:6TYK
ChainResidueDetails
BARG11
BPRO38
BSER39
BARG176
AARG11
APRO38
ASER39
AARG176

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:34748729, ECO:0007744|PDB:6PZ0, ECO:0007744|PDB:6TYK
ChainResidueDetails
ATYR72
ALYS92
BMET41
BGLU68
BTYR72
BLYS92
AMET41
AGLU68

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PDB entries from 2024-05-15

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