Research workbench
Fusion of maltose-binding protein and pila from acinetobacter nosocomialis M2
Analyse Fusion of maltose-binding protein and pila from acinetobacter nosocomialis M2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CFV
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic PROTEIN,MALTOSE-binding periplasmic PROTEIN,PILA fusion…
- UniProt
- P0AEX9
- Ligands
- GLC, MG
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic PROTEIN,MALTOSE-binding periplasmic PROTEIN,PILA fusion protein | protein | 484 | 43% helix, 22% strand | P0AEX9 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.69 | 0.82 | 34 | GLC |
| 2 | 216 | 0.68 | 0.85 | 36 | empty |
| 3 | 50 | 0.37 | 0.80 | 18 | GOL |
| 4 | 75 | 0.31 | 0.74 | 22 | empty |
| 5 | 58 | 0.28 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5CFV · Fusion of Maltose-binding Protein and PilA from Acinetobacter nosocomialis M2 · 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 P0AEX9
- Elsewhere: RCSB PDB 5CFV · PDBe 5CFV · UniProt P0AEX9
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