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2RIV

Crystal structure of the reactive loop cleaved human Thyroxine Binding Globulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ALYS287
AHOH514
AHIS336
AGLY338
AGLU339
ALYS340
AGLY341
AHOH414
AHOH416
AHOH448

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
ASER242
ALYS243
AASN244
AHOH445
BARG378

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 356
ChainResidue
APHE62
AGLN69
AGLN89
ALYS125
ATHR210
ATHR211
ATHR212
AHOH606

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 357
ChainResidue
ASER197
ATHR199
AGLU200
AASP201
AHOH717

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 358
ChainResidue
AGLN238
AASN273
AHOH404
AHOH629
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

237992

PDB entries from 2025-06-25

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