Research workbench
42F3 TCR PCPC5/H-2LD complex
Analyse 42F3 TCR PCPC5/H-2LD complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MXQ
- Type
- protein
- Length
- 621 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 42F3 alpha vmvh chimera; 42F3 beta vmvh chimera; H-2 class I histocompatibility antigen…
- UniProt
- P01897
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 14% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 42F3 alpha vmvh chimera | protein | 199 | 3% helix, 45% strand | — |
| D | 42F3 beta vmvh chimera | protein | 239 | 7% helix, 52% strand | — |
| A | H-2 class I histocompatibility antigen, L-D alpha chain | protein | 174 | 38% helix, 33% strand | P01897 |
| B | PCPC5 | protein | 9 | 0% helix, 0% strand | — |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.75 | 0.78 | 76 | empty |
| 2 | 340 | 0.66 | 0.81 | 57 | empty |
| 3 | 89 | 0.40 | 0.78 | 19 | empty |
| 4 | 78 | 0.34 | 0.75 | 17 | empty |
| 5 | 75 | 0.31 | 0.74 | 22 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2231 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 866 Ų buried · 17 hydrogen bonds · protein-protein
- D–A · 414 Ų buried · 3 hydrogen bonds · protein-protein
- C–A · 357 Ų buried · 6 hydrogen bonds · protein-protein
- D–B · 224 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P01897
- Elsewhere: RCSB PDB 4MXQ · PDBe 4MXQ · UniProt P01897
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