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7RLK

Wallaby TTR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006144biological_processpurine nucleobase metabolic process
A0007165biological_processsignal transduction
A0070324molecular_functionthyroid hormone binding
B0005179molecular_functionhormone activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006144biological_processpurine nucleobase metabolic process
B0007165biological_processsignal transduction
B0070324molecular_functionthyroid hormone binding
C0005179molecular_functionhormone activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006144biological_processpurine nucleobase metabolic process
C0007165biological_processsignal transduction
C0070324molecular_functionthyroid hormone binding
D0005179molecular_functionhormone activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006144biological_processpurine nucleobase metabolic process
D0007165biological_processsignal transduction
D0070324molecular_functionthyroid hormone binding
E0005179molecular_functionhormone activity
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006144biological_processpurine nucleobase metabolic process
E0007165biological_processsignal transduction
E0070324molecular_functionthyroid hormone binding
F0005179molecular_functionhormone activity
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0006144biological_processpurine nucleobase metabolic process
F0007165biological_processsignal transduction
F0070324molecular_functionthyroid hormone binding
Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGrPAvnVdV
ChainResidueDetails
ALYS15-VAL30

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSFS
ChainResidueDetails
ATYR105-SER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02766
ChainResidueDetails
ALYS15
DLYS15
DGLU54
AGLU54
BLYS15
BGLU54
CGLU54
ELYS15
EGLU54
FLYS15
FGLU54
ASER117
BSER117
CSER117
DSER117
ESER117
FSER117
CLYS15

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Sulfocysteine => ECO:0000250|UniProtKB:P02766
ChainResidueDetails
ACYS10
BCYS10
CCYS10
DCYS10
ECYS10
FCYS10

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000250|UniProtKB:P02766
ChainResidueDetails
AGLU42
BGLU42
CGLU42
DGLU42
EGLU42
FGLU42

221051

PDB entries from 2024-06-12

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