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7ERK

Crystal structure of V30M-TTR in complex with dasatinib

Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 1N1 A 201
ChainResidue
ALYS15
ALEU110
ASER117
ASER117
ATHR119
ATHR119
AVAL121
ALYS15
ALEU17
ALEU17
AGLU54
AHIS56
AALA108
AALA108
AALA109

site_idAC2
Number of Residues13
Detailsbinding site for residue 1N1 B 201
ChainResidue
BLYS15
BLEU17
BLEU17
BGLU54
BTHR106
BALA108
BALA108
BALA109
BLEU110
BLEU110
BSER117
BSER117
BTHR119

Functional Information from PROSITE/UniProt
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

222926

PDB entries from 2024-07-24

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