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5OQ0

Crystal structure of transthyretin mutant 87-110-117

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
ChainResidueDetails
ALYS15
AGLU54
AGLU117

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
ChainResidueDetails
ACYS10

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
ChainResidueDetails
AGLU42

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767
ChainResidueDetails
ASER52

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
ChainResidueDetails
AASN98

218853

PDB entries from 2024-04-24

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