Research workbench
Crystal structure of a prokaryotic sefir domain
Analyse Crystal structure of a prokaryotic sefir domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y8F
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sefir domain protein
- UniProt
- C2XMK4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sefir domain protein | protein | 144 | 49% helix, 15% strand | C2XMK4 |
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 | 319 | 0.66 | 0.81 | 42 | empty |
| 2 | 66 | 0.38 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 997 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5Y8F · Crystal Structure of a prokaryotic SEFIR 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
- Every structure of UniProt C2XMK4
- Elsewhere: RCSB PDB 5Y8F · PDBe 5Y8F · UniProt C2XMK4
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