› 1gq8

X-ray diffraction
1.75Å resolution

Pectin methylesterase from Carrot

Released:
DOI: 10.2210/pdb1gq8/pdb
PDB entry 1gq8 coloured by chain, front view.
PDB entry 1gq8 coloured by chain, side view.
PDB entry 1gq8 coloured by chain, top view.
Source organism: Daucus carota
Primary publication:
Crystal structure of plant pectin methylesterase.
Johansson K, El-Ahmad M, Friemann R, Jörnvall H, Markovic O, Eklund H
FEBS Lett 514 243-9 (2002)
PMID: 11943159

Function and Biology Details

Reaction catalysed: 
Pectin + n H(2)O = n methanol + pectate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pectinesterase Chain: A
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 34.23 KDa
Source organism: Daucus carota
UniProt:
  • Canonical: P83218 (Residues: 1-319; Coverage: 100%)
Sequence domains: Pectinesterase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

1 bound ligand:
Ligand CAC 2 x CAC
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21212
Unit cell:
a: 77.69Å b: 89.41Å c: 49.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.193

Quick links

Citations

4 review citations

Pectin methylesterase and its proteinaceous inhibitor: a review.
Jolie et al. (2010)
3 more

15 mentions without citation

Evidence for assembly of prions with left-handed beta-helices into trimers.
Govaerts et al. (2004)
14 more