Research workbench
Crystal structure of the human btla-hvem complex
Analyse Crystal structure of the human btla-hvem complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AW2
- Type
- protein
- Length
- 417 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- B and T lymphocyte attenuator; Tumor necrosis factor receptor superfamily member 14
- UniProt
- Q7Z6A9, Q92956
- Ligands
- NAG, FUL, NI
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 4% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B and T lymphocyte attenuator | protein | 110 | 5% helix, 52% strand | Q7Z6A9 |
| B, Y | Tumor necrosis factor receptor superfamily member 14 | protein | 100 | 3% helix, 42% strand | Q92956 |
| X | B and T lymphocyte attenuator | protein | 107 | 3% helix, 55% strand | Q7Z6A9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains B, Y
- FUL · beta-L-fucopyranose · sugar
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.73 | 0.96 | 28 | empty |
| 2 | 149 | 0.51 | 0.79 | 19 | empty |
| 3 | 153 | 0.49 | 0.78 | 31 | empty |
| 4 | 118 | 0.42 | 0.77 | 26 | empty |
| 5 | 89 | 0.40 | 0.78 | 19 | empty |
Interfaces
6 interfaces between chains.
- X–Y · 980 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 963 Ų buried · 23 hydrogen bonds · protein-protein
- A–X · 463 Ų buried · 7 hydrogen bonds · protein-protein
- A–Y · 210 Ų buried · 2 hydrogen bonds · protein-protein
- B–X · 197 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 2AW2 · Crystal structure of the human BTLA-HVEM complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q7Z6A9 · AlphaFold monomer V2.0 prediction for B- and T-lymphocyte attenuator (Q7Z6A9) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q92956 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member… · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q7Z6A9
- Every structure of UniProt Q92956
- Elsewhere: RCSB PDB 2AW2 · PDBe 2AW2 · UniProt Q7Z6A9 · UniProt Q92956
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