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Crystal structure of bacillus subtilis maf protein
Analyse Crystal structure of bacillus subtilis maf protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EX2
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein maf
- UniProt
- Q02169
- Ligands
- GLC, FRU, PO4
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein maf | protein | 185 | 36% helix, 26% strand | Q02169 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- FRU · beta-D-fructofuranose · sugar · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.56 | 0.77 | 40 | PO4 |
| 2 | 215 | 0.53 | 0.78 | 27 | PO4 |
| 3 | 201 | 0.53 | 0.78 | 21 | empty |
| 4 | 194 | 0.52 | 0.77 | 27 | empty |
| 5 | 73 | 0.40 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 599 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q02169
- Elsewhere: RCSB PDB 1EX2 · PDBe 1EX2 · UniProt Q02169
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