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1ETB

THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL 30-->MET VARIANT TO 1.7 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
10005179molecular_functionhormone activity
10005515molecular_functionprotein binding
10005576cellular_componentextracellular region
10005615cellular_componentextracellular space
10005737cellular_componentcytoplasm
10006144biological_processpurine nucleobase metabolic process
10007165biological_processsignal transduction
10035578cellular_componentazurophil granule lumen
10042802molecular_functionidentical protein binding
10070062cellular_componentextracellular exosome
10070324molecular_functionthyroid hormone binding
20005179molecular_functionhormone activity
20005515molecular_functionprotein binding
20005576cellular_componentextracellular region
20005615cellular_componentextracellular space
20005737cellular_componentcytoplasm
20006144biological_processpurine nucleobase metabolic process
20007165biological_processsignal transduction
20035578cellular_componentazurophil granule lumen
20042802molecular_functionidentical protein binding
20070062cellular_componentextracellular exosome
20070324molecular_functionthyroid hormone binding
Functional Information from PDB Data
site_idAA
Number of Residues7
DetailsT4 BINDING SITE COMPOSED OF RESIDUES FROM CHAIN 1 AND ITS 2-FOLD SYMMETRIC CHAIN. ONLY THE RESIDUES FROM CHAIN 1 ARE LISTED HERE
ChainResidue
1LYS15
1GLU54
1LEU17
1ALA108
1THR109
1LEU110
1SER117

site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE T44 1 128
ChainResidue
1MET13
1LYS15
1LEU17
1LEU17
1GLU54
1ALA108
1THR109
1LEU110
1LEU110
1HOH215

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE T44 2 129
ChainResidue
2LYS15
2LEU17
2GLU54
2ALA108
2THR109
2LEU110
2HOH211

site_idBB
Number of Residues7
DetailsT4 BINDING SITE COMPOSED OF RESIDUES FROM CHAIN 2 AND ITS 2-FOLD SYMMETRIC CHAIN. ONLY THE RESIDUES FROM CHAIN 1 ARE LISTED HERE
ChainResidue
2LEU17
2ALA108
2THR109
2LEU110
2SER117
2LYS15
2GLU54

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV
ChainResidueDetails
1LYS15-VAL30

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YTIAtlLSPYSYS
ChainResidueDetails
1TYR105-SER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
ChainResidueDetails
1LYS15
1GLU54
1SER117
2LYS15
2GLU54
2SER117

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
ChainResidueDetails
1CYS10
2CYS10

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
ChainResidueDetails
1GLU42
2GLU42

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767
ChainResidueDetails
1SER52
2SER52

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
ChainResidueDetails
1ASN98
2ASN98

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PDB entries from 2024-10-30

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