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4Y9B

Crystal structure of V30M mutated transthyretin in complex with alpha-mangostin

Functional Information from GO Data
ChainGOidnamespacecontents
A0042572biological_processretinol metabolic process
A0070324molecular_functionthyroid hormone binding
A0070327biological_processthyroid hormone transport
B0042572biological_processretinol metabolic process
B0070324molecular_functionthyroid hormone binding
B0070327biological_processthyroid hormone transport
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue MKS A 200
ChainResidue
ALYS15
ATHR119
ATHR119
AVAL121
ACL201
AHOH301
AHOH301
AHOH308
AHOH333
AHOH333
ALYS15
ALEU17
ATHR106
AALA108
AALA108
ALEU110
ASER117
ASER117

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 201
ChainResidue
AMKS200
AHOH301

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 202
ChainResidue
AGLU62
AGLU72
AHOH313
AHOH344

site_idAC4
Number of Residues19
Detailsbinding site for residue MKS B 200
ChainResidue
BLYS15
BLEU17
BTHR106
BALA108
BALA108
BLEU110
BLEU110
BSER117
BSER117
BTHR119
BTHR119
BVAL121
BCL201
BCL201
BHOH301
BHOH301
BHOH331
BHOH331
BHOH398

site_idAC5
Number of Residues4
Detailsbinding site for residue CL B 201
ChainResidue
BLYS15
BMKS200
BMKS200
BHOH301

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

219140

PDB entries from 2024-05-01

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