› 2nsp

X-ray diffraction
1.7Å resolution

Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide I

Released:
DOI: 10.2210/pdb2nsp/pdb
PDB entry 2nsp coloured by chain, front view.
PDB entry 2nsp coloured by chain, side view.
PDB entry 2nsp coloured by chain, top view.
Source organism: Dickeya dadantii 3937
Primary publication:
Molecular basis of the activity of the phytopathogen pectin methylesterase.
Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW
EMBO J 26 3879-87 (2007)
PMID: 17717531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Pectinesterase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 36.95 KDa
Source organism: Dickeya dadantii 3937
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C1A9 (Residues: 25-366; Coverage: 100%)
Gene names: Dda3937_03374, pem, pemA
Sequence domains: Pectinesterase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: M8C, ADA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 51.11Å b: 85.103Å c: 97.281Å
α: 90° β: 93.48° γ: 90°
R-values:
R R work R free
0.189 0.189 0.204
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The biochemistry and structural biology of plant cell wall deconstruction.
Gilbert HJ. (2010)
3 more

8 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
7 more