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4X30

Crystal structure of human Thyroxine-binding globulin complexed with thyroine at 1.55 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0070062cellular_componentextracellular exosome
A0070327biological_processthyroid hormone transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue T44 A 401
ChainResidue
ASER23
AHOH501
AHOH554
AHOH594
AHOH635
AGLU137
APHE139
ALEU269
ALYS270
AASN273
ALEU376
AGLU377
AARG378

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
ALEU206
AILE207
AASP208
AGLU254
AARG369
ASER370
AHOH820
AHOH853

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 403
ChainResidue
AASP28
APHE29
AASN32
ATHR75
AGLY77
AMET303
AHOH654
AHOH724

site_idAC4
Number of Residues4
Detailsbinding site for residue F A 404
ChainResidue
AALA191
AGLU351
ANA406
AHOH776

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
AARG36
AHOH657
AHOH724

site_idAC6
Number of Residues4
Detailsbinding site for residue NA A 406
ChainResidue
AALA191
AGLU351
AF404
AHOH747

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. IQIDRSFMLlI
ChainResidueDetails
AILE365-ILE375

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16938877","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Gary","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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