MolNFT v1 · #25298 · protein
Crystal structure of spore coat polysaccharide biosynthesis protein spse (BSU37870) from bacillus subtilis at 2.38 a resolution
1VLI: “Crystal structure of spore coat polysaccharide biosynthesis protein spse (BSU37870) from bacillus subtilis at…”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.69). MolNFT v1 #25298 on GenesisL1: 3D structure…
- PDB
- 1VLI
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat polysaccharide biosynthesis protein spse
- UniProt
- P39625
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat polysaccharide biosynthesis protein spse | protein | 358 | 35% helix, 18% strand | P39625 |
Ligands and binding sites
- ZN · Zinc ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.69 | 0.82 | 36 | ZN |
| 2 | 261 | 0.54 | 0.76 | 31 | empty |
| 3 | 77 | 0.38 | 0.77 | 19 | empty |
| 4 | 56 | 0.28 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1VLI · Crystal structure of Spore coat polysaccharide biosynthesis protein spsE (BSU37870) from… · the same entry in another collection · chain A against A, TM-score 1.00
- P39625 · AlphaFold monomer V2.0 prediction for spore coat polysaccharide biosynthesis protein spse… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P39625
- Elsewhere: RCSB PDB 1VLI · PDBe 1VLI · UniProt P39625
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