Research workbench
Crystal structure of alginate lyase A1-II' N141C/N199C
Analyse Crystal structure of alginate lyase A1-II' N141C/N199C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZA9
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate lyase
- EC
- 4.2.2.3
- UniProt
- Q75WP3
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alginate lyase (EC 4.2.2.3) | protein | 227 | 8% helix, 48% strand | Q75WP3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.44 | 0.76 | 28 | SO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2ZA9 · Crystal Structure of Alginate lyase A1-II' N141C/N199C · 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 Q75WP3
- Elsewhere: RCSB PDB 2ZA9 · PDBe 2ZA9 · UniProt Q75WP3
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