› 5a29

X-ray diffraction
1.9Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165422 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Exopolygalacturonate lyase Chain: A
Molecule details ›
Chain: A
Length: 570 amino acids
Theoretical weight: 64.68 KDa
Source organism: Vibrio vulnificus YJ016
UniProt:
  • Canonical: Q7MCK3 (Residues: 19-566; Coverage: 100%)
Gene name: VVA1383
Sequence domains: Periplasmic pectate lyase
Structure domains:
PECTATE LYASE Chain: B
Molecule details ›
Chain: B
Length: 18 amino acids
Theoretical weight: 2.04 KDa
Source organism: Vibrio vulnificus YJ016
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand MN 1 x MN
Ligand SRT 3 x SRT
Ligand EDO 12 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P65
Unit cell:
a: 141.102Å b: 141.102Å c: 72.426Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.156 0.197
Expression system: Not provided

Quick links

Citations

1 review citation

Polysaccharide Utilization Loci: Fueling Microbial Communities.
Grondin et al. (2017)
7 other articles

1 mention without citation

Functional Analyses of Resurrected and Contemporary Enzymes Illuminate an Evolutionary Path for the Emergence of Exolysis in Polysaccharide Lyase Family 2.
McLean et al. (2015)