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1DVX

CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC

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_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE DIF B 125
ChainResidue
ALYS15
ASER117
ATHR118
ATHR119
BLYS15
BLEU17
BLEU17
BALA108
BALA108
BLEU110
BLEU110
ALEU17
BSER117
BSER117
BTHR118
BTHR119
BTHR119
BVAL121
ALEU17
AALA108
AALA108
AALA109
ALEU110
ALEU110
ASER117

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

223790

PDB entries from 2024-08-14

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