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In-situ structure of hexameric S-layer protein
Analyse In-situ structure of hexameric S-layer protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PTT
- Type
- protein
- Length
- 4,350 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell surface glycoprotein
- UniProt
- P25062
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 9% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Cell surface glycoprotein | protein | 725 | 9% helix, 38% strand | P25062 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 973 | 0.72 | 0.77 | 112 | empty |
| 2 | 904 | 0.71 | 0.76 | 102 | empty |
| 3 | 824 | 0.70 | 0.76 | 94 | empty |
| 4 | 781 | 0.69 | 0.76 | 87 | empty |
| 5 | 632 | 0.63 | 0.74 | 75 | empty |
Interfaces
6 interfaces between chains.
- A–F · 1160 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1134 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1118 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 1113 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 1102 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 P25062
- Elsewhere: RCSB PDB 7PTT · PDBe 7PTT · UniProt P25062
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