Research workbench
Crystal structure of a designed protein
Analyse Crystal structure of a designed protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IEV
- Type
- protein
- Length
- 321 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Designed protein
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Designed protein | protein | 111 | 36% helix, 28% strand | — |
| B, C | Designed protein | protein | 105 | 39% helix, 30% 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 | 261 | 0.59 | 0.78 | 34 | empty |
| 2 | 148 | 0.43 | 0.75 | 23 | empty |
| 3 | 79 | 0.32 | 0.74 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 549 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 380 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 252 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6IEV · Crystal structure of a designed protein · 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 6IEV · PDBe 6IEV
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