Research workbench
Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors
Analyse Different thermodynamic binding mechanisms and peptide fine specificities… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ERY
- Type
- protein
- Length
- 341 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q02218
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 174 | — | — |
| B | — | protein | 149 | — | — |
| P, Q | — | protein | 9 | — | Q02218 |
Compared structures
- 3ERY · Different thermodynamic binding mechanisms and peptide fine specificities associated with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q02218 · AlphaFold monomer V2.0 prediction for 2-oxoglutarate dehydrogenase, mitochondrial (Q02218) · a predicted model of the same protein · chain P against A, TM-score 0.35
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q02218
- Elsewhere: RCSB PDB 3ERY · PDBe 3ERY · UniProt Q02218
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