MolNFT v1 · #91500 · protein
Structure basis of a novel virulence factor ghip a glycosyl hydrolase 25 of streptococcus pneumoniae participating in host cell invasion
4FF5: “Structure basis of a novel virulence factor ghip a glycosyl hydrolase 25 of streptococcus pneumoniae…”. X-ray diffraction, 3 pockets (best druggability 0.40). MolNFT v1 #91500 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4FF5
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase 25
- UniProt
- Q97R47
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase 25 | protein | 227 | 33% helix, 22% strand | Q97R47 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.40 | 0.79 | 16 | empty |
| 2 | 90 | 0.37 | 0.76 | 18 | empty |
| 3 | 74 | 0.33 | 0.75 | 22 | EDO |
Compared structures
- 4FF5 · Structure basis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus… · 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 Q97R47
- Elsewhere: RCSB PDB 4FF5 · PDBe 4FF5 · UniProt Q97R47
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