Research workbench
Zn-mediated trimer of maltose-binding protein E310H/K314H by synthetic symmetrization
Analyse Zn-mediated trimer of maltose-binding protein E310H/K314H by synthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SEV
- Type
- protein
- Length
- 1,110 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein
- UniProt
- P0AEX9
- Ligands
- GLC, ZN, CL
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Maltose-binding periplasmic protein | protein | 370 | 44% helix, 21% strand | P0AEX9 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, C, E
- ZN · Zinc ion · metal · 3 copies · chains A, C, E
- CL · Chloride ion · ion · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.82 | 0.85 | 77 | CL |
| 2 | 328 | 0.71 | 0.84 | 35 | GLC |
| 3 | 330 | 0.70 | 0.83 | 33 | GLC |
| 4 | 331 | 0.68 | 0.82 | 35 | GLC |
| 5 | 376 | 0.65 | 0.79 | 48 | empty |
Interfaces
3 interfaces between chains.
- C–E · 682 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 676 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 633 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3SEV · Zn-mediated Trimer of Maltose-binding Protein E310H/K314H by Synthetic Symmetrization · 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 3SEV · PDBe 3SEV · UniProt P0AEX9
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