Research workbench
Crystal structure of sphingomonas sp. A1 alginate-binding protein ALGQ1 in complex with saturated trimannuronate
Analyse Crystal structure of sphingomonas sp. A1 alginate-binding protein ALGQ1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VLU
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALGQ1
- UniProt
- Q9KWT6
- Ligands
- BEM, CA
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALGQ1 | protein | 490 | 46% helix, 15% strand | Q9KWT6 |
Ligands and binding sites
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 | 1064 | 0.82 | 0.84 | 90 | BEM |
| 2 | 67 | 0.31 | 0.74 | 24 | empty |
Compared structures
- 3VLU · Crystal structure of Sphingomonas sp. A1 alginate-binding protein AlgQ1 in complex with… · 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 Q9KWT6
- Elsewhere: RCSB PDB 3VLU · PDBe 3VLU · UniProt Q9KWT6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.