Research workbench
Crystal structure of the periplasmic chaperone skp
Analyse Crystal structure of the periplasmic chaperone skp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SG2
- Type
- protein
- Length
- 392 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Seventeen kilodalton protein
- UniProt
- P0AEU7
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Seventeen kilodalton protein | protein | 141 | 67% helix, 10% strand | P0AEU7 |
| B | Seventeen kilodalton protein | protein | 109 | 62% helix, 13% strand | P0AEU7 |
| C | Seventeen kilodalton protein | protein | 142 | 74% helix, 9% strand | P0AEU7 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.40 | 0.78 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 944 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 549 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 548 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 P0AEU7
- Elsewhere: RCSB PDB 1SG2 · PDBe 1SG2 · UniProt P0AEU7
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