› 6szo

X-ray diffraction
2.2Å resolution

The glucuronoyl esterase OtCE15A S267A variant from Opitutus terrae in complex with D-galacturonate

Released:
DOI: 10.2210/pdb6szo/pdb
PDB entry 6szo coloured by chain, front view.
PDB entry 6szo coloured by chain, side view.
PDB entry 6szo coloured by chain, top view.
Source organism: Opitutus terrae PB90-1
Primary publication:
Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components.
Mazurkewich S, Poulsen JN, Lo Leggio L, Larsbrink J
J Biol Chem 294 19978-19987 (2019)
PMID: 31740581

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative acetyl xylan esterase Chain: A
Molecule details ›
Chain: A
Length: 421 amino acids
Theoretical weight: 46.13 KDa
Source organism: Opitutus terrae PB90-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B1ZMF4 (Residues: 33-432; Coverage: 96%)
Gene name: Oter_0116

Ligands and Environments

6 bound ligands:
Ligand GTR 1 x GTR
Ligand DMS 4 x DMS
Ligand MG 1 x MG
Ligand EDO 24 x EDO
Ligand PEG 4 x PEG
Ligand PGE 4 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P1
Unit cell:
a: 44.626Å b: 46.138Å c: 50.195Å
α: 63.653° β: 86.794° γ: 71.166°
R-values:
R R work R free
0.159 0.154 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.
Larsbrink et al. (2023)
1 more

1 mention without citation

Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components.
Mazurkewich et al. (2019)