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Crystal structure of aal mutant H59Q complex with lactose
Analyse Crystal structure of aal mutant H59Q complex with lactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZGO
- Type
- protein
- Length
- 333 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-tumor lectin
- EC
- 3.1.21.-
- UniProt
- Q6WY08
- Ligands
- BGC, GAL
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-tumor lectin (EC 3.1.21.-) | protein | 167 | 3% helix, 53% strand | Q6WY08 |
| B | Anti-tumor lectin (EC 3.1.21.-) | protein | 166 | 3% helix, 54% strand | Q6WY08 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
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 | 165 | 0.53 | 0.79 | 28 | empty |
| 2 | 52 | 0.45 | 0.84 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1452 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
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 Q6WY08
- Elsewhere: RCSB PDB 2ZGO · PDBe 2ZGO · UniProt Q6WY08
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