1j1t

X-ray diffraction
2Å resolution

Alginate lyase from Alteromonas sp.272

Released:
Source organism: Alteromonas sp. 272
Entry authors: Motoshima H, Iwatomo Y, Watanabe K, Oda T, Muramatsu T

Function and Biology Details

Reaction catalysed:
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-551297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alginate lyase 2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 25.58 KDa
Source organism: Alteromonas sp. 272
UniProt:
  • Canonical: P84143 (Residues: 1-233; Coverage: 100%)
Sequence domains: Alginate lyase
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P6122
Unit cell:
a: 46.2Å b: 46.2Å c: 387.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.248