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1IIK

CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLLECTED AT CRYO TEMPERATURE

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 Residues6
DetailsBINDING SITE FOR RESIDUE BME A 901
ChainResidue
APHE87
ACYS114
AHOH959
BARG21
BALA120
BVAL122

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 902
ChainResidue
BPRO113
BCYS114
AHOH953
BPRO86
BPHE87

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 903
ChainResidue
AALA108
ASER117
ATHR118
ATHR119
ABME904
ABME904

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 904
ChainResidue
AALA108
ASER117
ATHR118
ATHR119
ABME903
ABME903

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 905
ChainResidue
BSER117
BTHR118
BTHR119
BBME906
BBME906

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 906
ChainResidue
BSER117
BTHR118
BTHR119
BBME905
BBME905

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
ChainResidueDetails
ALYS15
AGLU54
ASER117
BLYS15
BGLU54
BSER117

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
ChainResidueDetails
ACYS10
BCYS10

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
ChainResidueDetails
AGLU42
BGLU42

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767
ChainResidueDetails
ASER52
BSER52

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
ChainResidueDetails
AASN98
BASN98

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PDB entries from 2024-07-03

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