Research workbench
T cell receptor VALPHA11 (AV11S5) domain
Analyse T cell receptor VALPHA11 (AV11S5) domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H5B
- Type
- protein
- Length
- 448 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Murine T cell receptor (TCR) valpha domain
- Ligands
- CL
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Murine T cell receptor (TCR) valpha domain | protein | 113 | 3% helix, 53% strand | — |
| B, D | Murine T cell receptor (TCR) valpha domain | protein | 111 | 3% helix, 56% strand | — |
| C | Murine T cell receptor (TCR) valpha domain | protein | 113 | 3% helix, 58% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 802 | 0.73 | 0.78 | 65 | empty |
| 2 | 179 | 0.51 | 0.78 | 21 | empty |
| 3 | 132 | 0.43 | 0.76 | 18 | empty |
| 4 | 57 | 0.27 | 0.74 | 14 | empty |
Interfaces
5 interfaces between chains.
- A–B · 886 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 717 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 176 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 167 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 42 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1H5B · T cell receptor Valpha11 (AV11S5) domain · 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 1H5B · PDBe 1H5B
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