Research workbench
Crystal structure of the T33-51H designed self-assembling protein tetrahedron
Analyse Crystal structure of the T33-51H designed self-assembling protein tetrahedron in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CY5
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T33-51H-B; T33-51H-a
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | T33-51H-B | protein | 149 | 74% helix, 3% strand | — |
| A | T33-51H-a | protein | 137 | 80% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.52 | 0.77 | 27 | empty |
| 2 | 243 | 0.46 | 0.73 | 30 | empty |
| 3 | 71 | 0.36 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- B–A · 689 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5CY5 · Crystal structure of the T33-51H designed self-assembling protein tetrahedron · the same entry in another collection · chain B against B, 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 5CY5 · PDBe 5CY5
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