Research workbench
Crystal structure of paradendryphiella salina PL7A alginate lyase in complex with tri-mannuronic acid
Analyse Crystal structure of paradendryphiella salina PL7A alginate lyase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OOF
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate lyase (PL7)
- UniProt
- A0A485PVH1
- Ligands
- MAV, BEM
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alginate lyase (PL7) | protein | 226 | 8% helix, 58% strand | A0A485PVH1 |
Ligands and binding sites
- MAV · alpha-D-mannopyranuronic acid · ligand · chains A
- BEM · beta-D-mannopyranuronic acid · sugar · 3 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7OOF · Crystal structure of Paradendryphiella salina PL7A alginate lyase in complex with… · 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 A0A485PVH1
- Elsewhere: RCSB PDB 7OOF · PDBe 7OOF · UniProt A0A485PVH1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.