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2XN6

Crystal structure of thyroxine-binding globulin complexed with thyroxine-fluoresein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 1356
ChainResidue
AGLN109
AHIS185
AHOH2033

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1357
ChainResidue
AARG355
ALYS118
ALEU120
AASN312
AALA313
AASP314
AASN322

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1358
ChainResidue
APHE29
AASN32
ATHR75
AGLY77
AMET303
AHOH2284
AHOH2285

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1396
ChainResidue
AASP43
AMET257
BSER370
BLYS388
BHOH2018

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1359
ChainResidue
AGLN220
AASP222
AASP222
AHOH2154
AHOH2155
AHOH2184

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1360
ChainResidue
ALYS287
AHIS336
AGLY338
AGLU339
ALYS340
AGLY341
AEDO1364

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1361
ChainResidue
AVAL39
AGLU40
AILE146
ALYS150
AASP171
ALEU172

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1362
ChainResidue
ALYS118
APHE143
AHOH2096
AHOH2116

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1363
ChainResidue
AALA292
ATHR293
ATYR294
AHOH2030

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1364
ChainResidue
AALA188
AGLN189
ATHR342
AGLU343
AEDO1360
AHOH2281

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 1365
ChainResidue
ASER140
AGLU320
AASP321

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 1366
ChainResidue
AASN312

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE F6Y A 1369
ChainResidue
AGLU105
ATYR225
AASN273
AT441370
AHOH2225

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE T44 A 1370
ChainResidue
ASER23
AGLN238
ALEU246
ALEU269
ALYS270
AASN273
AF6Y1369
AHOH2287
BLEU376
BARG378

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. IQIDRSFMLlI
ChainResidueDetails
BILE365-ILE375

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16938877
ChainResidueDetails
BARG378

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN16

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN79
AASN233

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Gary => ECO:0000305
ChainResidueDetails
AILE96

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN145

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PDB entries from 2024-07-24

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