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1THA

MECHANISM OF MOLECULAR RECOGNITION. STRUCTURAL ASPECTS OF 3,3'-DIIODO-L-THYRONINE BINDING TO HUMAN SERUM TRANSTHYRETIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0006144biological_processpurine nucleobase metabolic process
A0007165biological_processsignal transduction
A0035578cellular_componentazurophil granule lumen
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A0070324molecular_functionthyroid hormone binding
B0005179molecular_functionhormone activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0006144biological_processpurine nucleobase metabolic process
B0007165biological_processsignal transduction
B0035578cellular_componentazurophil granule lumen
B0042802molecular_functionidentical protein binding
B0070062cellular_componentextracellular exosome
B0070324molecular_functionthyroid hormone binding
Functional Information from PDB Data
site_idA1
Number of Residues13
Details
ChainResidue
ALYS15
ATHR118
ATHR119
AALA120
AVAL121
AVAL16
ALEU17
ATHR106
AILE107
AALA108
AALA109
ALEU110
ASER117

site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE T33 A 130
ChainResidue
ALYS15
ALYS15
ALEU17
ATHR106
AALA108
AALA109
ALEU110
ASER117
ASER117

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE T33 B 130
ChainResidue
BLYS15
BLEU17
BALA108
BLEU110
BSER117
BSER117
BTHR118
BTHR119

site_idB1
Number of Residues13
Details
ChainResidue
BLYS15
BVAL16
BLEU17
BTHR106
BILE107
BALA108
BALA109
BLEU110
BSER117
BTHR118
BTHR119
BALA120
BVAL121

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV
ChainResidueDetails
ALYS15-VAL30

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS
ChainResidueDetails
ATYR105-SER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
ChainResidueDetails
ALYS35
AASP74
BLYS35
BASP74

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
ChainResidueDetails
AVAL30
BVAL30

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
ChainResidueDetails
AGLU62
BGLU62

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767
ChainResidueDetails
AGLU72
BGLU72

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
ChainResidueDetails
ATHR118
BTHR118

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PDB entries from 2024-03-27

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