MolNFT v1 · #20154 · protein
Evidence that structural rearrangements AND/OR flexibility during TCR binding can contribute to T-cell activation
1R5V: “Evidence that structural rearrangements AND/OR flexibility during TCR binding can contribute to T-cell…”. X-ray diffraction. MolNFT v1 #20154 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1R5V
- Type
- protein
- Length
- 756 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04224, P18468
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 180 | — | P04224 |
| E, F | — | protein | 13 | — | — |
| B, D | — | protein | 185 | — | P18468 |
Compared structures
- 1R5V · Evidence that structural rearrangements and/or flexibility during TCR binding can… · the same entry in another collection · chain D against D, TM-score 1.00
- P04224 · AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen, E-K alpha… · a predicted model of the same protein · chain A against A, TM-score 0.96
- P18468 · AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen, I-a beta… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P04224
- Every structure of UniProt P18468
- Elsewhere: RCSB PDB 1R5V · PDBe 1R5V · UniProt P04224 · UniProt P18468
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