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Crystal structure of family 7 alginate lyase A1-II' H191N/Y284F in complex with substrate (ggmg)
Analyse Crystal structure of family 7 alginate lyase A1-II' H191N/Y284F in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZAA
- Type
- protein
- Length
- 232 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
- LGU, MAW, BEM
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alginate lyase (EC 4.2.2.3) | protein | 232 | 7% helix, 50% strand | Q75WP3 |
Ligands and binding sites
- LGU · alpha-L-gulopyranuronic acid · ligand · 2 copies · chains A
- MAW · 4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid · ligand · chains A
- BEM · beta-D-mannopyranuronic acid · sugar · chains A
- GOL · Glycerol · additive · 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 | 190 | 0.49 | 0.76 | 30 | LGU, BEM, MAW |
Compared structures
- 2ZAA · Crystal Structure of Family 7 Alginate Lyase A1-II' H191N/Y284F in Complex with Substrate… · 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 2ZAA · PDBe 2ZAA · UniProt Q75WP3
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