Research workbench
Structure of a high-affinity mutant of the 2C TCR in complex with LD/QL9
Analyse Structure of a high-affinity mutant of the 2C TCR in complex with LD/QL9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E7L
- Type
- protein
- Length
- 814 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytotoxic tcell receptor; Beta-chain; H-2 class I histocompatibility antigen, L-D alpha…
- UniProt
- A2NTU7, A2NTY6, P01897
- Pockets
- 9 · best druggability 0.65
Structure
x-ray diffraction · 5 distinct chains · 15% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytotoxic tcell receptor | protein | 112 | 3% helix, 49% strand | A2NTU7 |
| B | Cytotoxic tcell receptor | protein | 110 | 3% helix, 53% strand | A2NTU7 |
| C, D | Beta-chain | protein | 112 | 3% helix, 51% strand | A2NTY6 |
| E, F | H-2 class I histocompatibility antigen, L-D alpha chain | protein | 175 | 38% helix, 32% strand | P01897 |
| P, Q | Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) | protein | 9 | 0% helix, 0% strand | — |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.65 | 0.78 | 56 | empty |
| 2 | 468 | 0.64 | 0.77 | 55 | empty |
| 3 | 356 | 0.54 | 0.74 | 32 | empty |
| 4 | 82 | 0.43 | 0.80 | 22 | empty |
| 5 | 96 | 0.42 | 0.78 | 23 | empty |
Interfaces
15 interfaces between chains.
- E–Q · 936 Ų buried · 13 hydrogen bonds · protein-protein
- F–P · 935 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 909 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 776 Ų buried · 7 hydrogen bonds · protein-protein
- A–E · 537 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2E7L · Structure of a high-affinity mutant of the 2C TCR in complex with Ld/QL9 · the same entry in another collection · chain Q against Q, TM-score 1.00
- P01897 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, L-D alpha… · a predicted model of the same protein · chain E against A, TM-score 0.99
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 A2NTU7
- Every structure of UniProt A2NTY6
- Every structure of UniProt P01897
- Elsewhere: RCSB PDB 2E7L · PDBe 2E7L · UniProt A2NTU7 · UniProt A2NTY6 · UniProt P01897
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