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
| Chain | GOid | namespace | contents |
| 1 | 0001523 | biological_process | retinoid metabolic process |
| 1 | 0005179 | molecular_function | hormone activity |
| 1 | 0005515 | molecular_function | protein binding |
| 1 | 0005576 | cellular_component | extracellular region |
| 1 | 0005615 | cellular_component | extracellular space |
| 1 | 0005737 | cellular_component | cytoplasm |
| 1 | 0006144 | biological_process | purine nucleobase metabolic process |
| 1 | 0007165 | biological_process | signal transduction |
| 1 | 0032991 | cellular_component | protein-containing complex |
| 1 | 0035578 | cellular_component | azurophil granule lumen |
| 1 | 0042562 | molecular_function | hormone binding |
| 1 | 0042802 | molecular_function | identical protein binding |
| 1 | 0044877 | molecular_function | protein-containing complex binding |
| 1 | 0070062 | cellular_component | extracellular exosome |
| 1 | 0140313 | molecular_function | molecular sequestering activity |
| 2 | 0001523 | biological_process | retinoid metabolic process |
| 2 | 0005179 | molecular_function | hormone activity |
| 2 | 0005515 | molecular_function | protein binding |
| 2 | 0005576 | cellular_component | extracellular region |
| 2 | 0005615 | cellular_component | extracellular space |
| 2 | 0005737 | cellular_component | cytoplasm |
| 2 | 0006144 | biological_process | purine nucleobase metabolic process |
| 2 | 0007165 | biological_process | signal transduction |
| 2 | 0032991 | cellular_component | protein-containing complex |
| 2 | 0035578 | cellular_component | azurophil granule lumen |
| 2 | 0042562 | molecular_function | hormone binding |
| 2 | 0042802 | molecular_function | identical protein binding |
| 2 | 0044877 | molecular_function | protein-containing complex binding |
| 2 | 0070062 | cellular_component | extracellular exosome |
| 2 | 0140313 | molecular_function | molecular sequestering activity |
Functional Information from PDB Data
| site_id | AA |
| Number of Residues | 7 |
| Details | T4 BINDING SITE COMPOSED OF RESIDUES FROM CHAIN 1 AND ITS 2-FOLD SYMMETRIC CHAIN. ONLY THE RESIDUES FROM CHAIN 1 ARE LISTED HERE |
| Chain | Residue |
| 1 | LYS15 |
| 1 | GLU54 |
| 1 | LEU17 |
| 1 | ALA108 |
| 1 | THR109 |
| 1 | LEU110 |
| 1 | SER117 |
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE T44 1 128 |
| Chain | Residue |
| 1 | MET13 |
| 1 | LYS15 |
| 1 | LEU17 |
| 1 | LEU17 |
| 1 | GLU54 |
| 1 | ALA108 |
| 1 | THR109 |
| 1 | LEU110 |
| 1 | LEU110 |
| 1 | HOH215 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE T44 2 129 |
| Chain | Residue |
| 2 | LYS15 |
| 2 | LEU17 |
| 2 | GLU54 |
| 2 | ALA108 |
| 2 | THR109 |
| 2 | LEU110 |
| 2 | HOH211 |
| site_id | BB |
| Number of Residues | 7 |
| Details | T4 BINDING SITE COMPOSED OF RESIDUES FROM CHAIN 2 AND ITS 2-FOLD SYMMETRIC CHAIN. ONLY THE RESIDUES FROM CHAIN 1 ARE LISTED HERE |
| Chain | Residue |
| 2 | LEU17 |
| 2 | ALA108 |
| 2 | THR109 |
| 2 | LEU110 |
| 2 | SER117 |
| 2 | LYS15 |
| 2 | GLU54 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11418763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ICT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Sulfocysteine","evidences":[{"source":"PubMed","id":"17175208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H4E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"4-carboxyglutamate; in a patient with Moyamoya disease","evidences":[{"source":"PubMed","id":"18221012","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02767","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






