Research workbench
B. fragilis nanu
Analyse B. fragilis nanu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L7T
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nanu sialic acid binding protein
- UniProt
- Q5LEN2
- Ligands
- NA
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nanu sialic acid binding protein | protein | 490 | 51% helix, 8% strand | Q5LEN2 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.72 | 0.98 | 24 | empty |
| 2 | 52 | 0.43 | 0.83 | 12 | empty |
| 3 | 70 | 0.30 | 0.74 | 14 | empty |
| 4 | 74 | 0.30 | 0.73 | 11 | empty |
Compared structures
- 4L7T · B. fragilis NanU · 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 Q5LEN2
- Elsewhere: RCSB PDB 4L7T · PDBe 4L7T · UniProt Q5LEN2
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