MolNFT v1 · #15408 · protein
Engineered high-affinity maltose-binding protein
1N3W · Maltose-binding periplasmic protein: “Engineered high-affinity maltose-binding protein”. X-ray diffraction, 1 ligand (GLC), 2 pockets (best druggability 0.71). MolNFT v1 #15408 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1N3W
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein
- UniProt
- P02928
- Ligands
- GLC
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein | protein | 366 | 43% helix, 17% strand | P02928 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.71 | 0.85 | 30 | GLC |
| 2 | 57 | 0.29 | 0.74 | 14 | empty |
Compared structures
- 1N3W · Engineered High-Affinity 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 1N3W · PDBe 1N3W · UniProt P02928
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