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Crystal structure of ALG17C mutant H202L
Analyse Crystal structure of ALG17C mutant H202L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OK4
- Type
- protein
- Length
- 1,409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative alginate lyase
- UniProt
- Q21FJ0
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative alginate lyase | protein | 704 | 35% helix, 28% strand | Q21FJ0 |
| B | Putative alginate lyase | protein | 705 | 35% helix, 28% strand | Q21FJ0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 663 | 0.80 | 0.85 | 81 | empty |
| 2 | 696 | 0.80 | 0.84 | 88 | empty |
| 3 | 1080 | 0.74 | 0.77 | 79 | empty |
| 4 | 107 | 0.45 | 0.79 | 36 | empty |
| 5 | 78 | 0.37 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2671 Ų buried · 56 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 Q21FJ0
- Elsewhere: RCSB PDB 4OK4 · PDBe 4OK4 · UniProt Q21FJ0
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