Research workbench
Crystal structure of MALE31, a defective folding mutant of maltose-binding protein
Analyse Crystal structure of MALE31, a defective folding mutant of maltose-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LAX
- Type
- protein
- Length
- 737 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Escherichia coli
- Molecule
- Maltose-binding protein mutant MALE31
- UniProt
- P02928
- Ligands
- GLC
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · resolution 1.85 · 2 distinct chains · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding protein mutant MALE31 | protein | 369 | 46% helix, 20% strand | P02928 |
| C | Maltose-binding protein mutant MALE31 | protein | 368 | 46% helix, 20% strand | P02928 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.71 | 0.85 | 29 | GLC |
| 2 | 302 | 0.70 | 0.84 | 33 | GLC |
| 3 | 353 | 0.62 | 0.78 | 46 | empty |
| 4 | 151 | 0.46 | 0.76 | 30 | empty |
Interfaces
1 interface between chains.
- A–C · 330 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1LAX · Crystal structure of MALE31, a defective folding mutant of maltose- binding protein · 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 P02928
- Elsewhere: RCSB PDB 1LAX · PDBe 1LAX · UniProt P02928
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