Research workbench
In-situ structure of pentameric S-layer protein
Analyse In-situ structure of pentameric 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
- 7PTP
- Type
- protein
- Length
- 3,625 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell surface glycoprotein
- UniProt
- P25062
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · 1 distinct chain · 9% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Cell surface glycoprotein | protein | 725 | 9% helix, 38% strand | P25062 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 907 | 0.74 | 0.78 | 94 | empty |
| 2 | 585 | 0.71 | 0.80 | 67 | empty |
| 3 | 607 | 0.71 | 0.79 | 70 | empty |
| 4 | 625 | 0.71 | 0.79 | 62 | empty |
| 5 | 599 | 0.69 | 0.78 | 65 | empty |
Interfaces
10 interfaces between chains.
- A–E · 1348 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 1317 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1236 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1204 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 1127 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 7PTP · PDBe 7PTP · UniProt P25062
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