Research workbench
Crystal structure of bacterial cell-surface alginate-binding protein ALGP7
Analyse Crystal structure of bacterial cell-surface alginate-binding protein ALGP7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AT7
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate-binding flagellin
- UniProt
- Q25C86
- Pockets
- 2 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alginate-binding flagellin | protein | 251 | 75% helix, 1% strand | Q25C86 |
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 | 1045 | 0.85 | 0.86 | 89 | empty |
| 2 | 90 | 0.35 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 885 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3AT7 · Crystal structure of bacterial cell-surface alginate-binding protein Algp7 · 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 Q25C86
- Elsewhere: RCSB PDB 3AT7 · PDBe 3AT7 · UniProt Q25C86
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