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1E4H

Structure of human transthyretin complexed with bromophenols: a new mode of binding

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 Residues12
DetailsBINDING SITE FOR RESIDUE PBR A 998
ChainResidue
AHOH2084
BTHR119
BHOH2058
BHOH2058
AHOH2084
BLYS15
BLYS15
BLEU17
BLEU17
BALA108
BALA108
BTHR119

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PBR B 999
ChainResidue
ALYS15
ALYS15
ATHR119
ATHR119

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 990
ChainResidue
ATRP41
ALYS70
AGLU72

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GOL B 990
ChainResidue
ALEU110
ASER117
ASER117
AHOH2077
AHOH2077
BLEU110
BLEU111
BSER112
BSER115
BTYR116
BSER117
BHOH2067
BHOH2067
BHOH2068

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 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

218853

PDB entries from 2024-04-24

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