Research workbench
Crystal structure of QW9-HLA-B*5301 specific T cell receptor, C3
Analyse Crystal structure of QW9-HLA-B*5301 specific T cell receptor, C3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R7Z
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha chain of C3 TCR; Beta chain of C3 TCR
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha chain of C3 TCR | protein | 203 | 6% helix, 45% strand | — |
| B | Beta chain of C3 TCR | protein | 242 | 7% helix, 49% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 927 | 0.70 | 0.75 | 78 | empty |
| 2 | 58 | 0.30 | 0.75 | 13 | SO4 |
Interfaces
1 interface between chains.
- A–B · 2371 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7R7Z · Crystal structure of QW9-HLA-B*5301 specific T Cell Receptor, C3 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7R7Z · PDBe 7R7Z
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