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6SCJ

The structure of human thyroglobulin

Functional Information from PROSITE/UniProt
site_idPS00484
Number of Residues31
DetailsTHYROGLOBULIN_1_1 Thyroglobulin type-1 repeat signature. YvpqCaed.GsFqtvQcqndgrsc....WCVgangS
ChainResidueDetails
ATYR48-SER78
ATYR116-GLY145
ATYR315-GLY343
APHE616-GLY643
APHE683-GLY710
ATYR1027-GLY1057
APHE1104-GLY1132
ATYR1165-GLY1195
AALA1519-GLY1548

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVFiP
ChainResidueDetails
AGLU2279-PRO2289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:8615697
ChainResidueDetails
AASN110
AASN496
AASN1869
AASN2122
BASN110
BASN496
BASN1869
BASN2122

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: Triiodothyronine; alternate => ECO:0000269|PubMed:2760035
ChainResidueDetails
ATYR24
ATYR704
ATYR2573
ATYR2766
BTYR24
BTYR704
BTYR2573
BTYR2766

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Iodotyrosine => ECO:0000305|PubMed:32025030
ChainResidueDetails
ATYR108
ATYR234
ATYR2540
BTYR108
BTYR234
BTYR2540

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Iodotyrosine; alternate => ECO:0000269|PubMed:2760035, ECO:0000305|PubMed:32025030
ChainResidueDetails
ATYR149
BTYR149

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: Iodotyrosine => ECO:0000269|PubMed:2760035
ChainResidueDetails
ATYR258
BTYR2617
ATYR785
ATYR2184
ATYR2587
ATYR2617
BTYR258
BTYR785
BTYR2184
BTYR2587

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Iodotyrosine; alternate => ECO:0000269|PubMed:2760035
ChainResidueDetails
ATYR869
ATYR992
ATYR1467
BTYR869
BTYR992
BTYR1467

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Diiodotyrosine => ECO:0000269|PubMed:2760035
ChainResidueDetails
ATYR883
ATYR2697
BTYR883
BTYR2697

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Thyroxine => ECO:0000269|PubMed:2760035, ECO:0000305|PubMed:32025030
ChainResidueDetails
ATYR1310
BTYR1310

site_idSWS_FT_FI9
Number of Residues26
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:32025030, ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ
ChainResidueDetails
AASN76
AASN2013
AASN2250
AASN2295
AASN2582
BASN76
BASN198
BASN484
BASN947
BASN1220
BASN1349
AASN198
BASN1365
BASN1716
BASN1774
BASN2013
BASN2250
BASN2295
BASN2582
AASN484
AASN947
AASN1220
AASN1349
AASN1365
AASN1716
AASN1774

site_idSWS_FT_FI10
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ
ChainResidueDetails
AASN110
AASN1869
AASN2122
BASN110
BASN1869
BASN2122

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8615697
ChainResidueDetails
AASN529
AASN748
AASN816
BASN529
BASN748
BASN816

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:8615697
ChainResidueDetails
AASN1348
BASN1348

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine => ECO:0000269|PubMed:16679516
ChainResidueDetails
ASER2749
BSER2749

227344

PDB entries from 2024-11-13

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