Research workbench
Computationally designed symmetric homotetramer
Analyse Computationally designed symmetric homotetramer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KWD
- Type
- protein
- Length
- 637 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ankyrin repeat-containing protein
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ankyrin repeat-containing protein | protein | 160 | 55% helix, 0% strand | — |
| C | Ankyrin repeat-containing protein | protein | 158 | 55% helix, 0% strand | — |
| D | Ankyrin repeat-containing protein | protein | 159 | 55% helix, 0% strand | — |
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 | 493 | 0.62 | 0.76 | 55 | empty |
| 2 | 232 | 0.46 | 0.74 | 32 | empty |
Interfaces
3 interfaces between chains.
- A–D · 537 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 536 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 256 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5KWD · Computationally Designed Symmetric Homotetramer · 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 5KWD · PDBe 5KWD
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