Research workbench
Alginate lyase A1-III H192A apo form
Analyse Alginate lyase A1-III H192A apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E1Y
- Type
- protein
- Length
- 706 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate lyase
- EC
- 4.2.2.3
- UniProt
- Q9KWU1
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alginate lyase (EC 4.2.2.3) | protein | 353 | 55% helix, 2% strand | Q9KWU1 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.67 | 0.78 | 48 | empty |
| 2 | 287 | 0.59 | 0.78 | 37 | empty |
| 3 | 148 | 0.46 | 0.76 | 26 | empty |
| 4 | 111 | 0.41 | 0.76 | 16 | empty |
| 5 | 105 | 0.40 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 340 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4E1Y · Alginate lyase A1-III H192A apo form · 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 Q9KWU1
- Elsewhere: RCSB PDB 4E1Y · PDBe 4E1Y · UniProt Q9KWU1
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