› 3wdt

X-ray diffraction
1.98Å resolution

The apo-form structure of PtLic16A from Paecilomyces thermophila

Released:
DOI: 10.2210/pdb3wdt/pdb
PDB entry 3wdt coloured by chain, front view.
PDB entry 3wdt coloured by chain, side view.
PDB entry 3wdt coloured by chain, top view.
Source organism: Paecilomyces sp. 'thermophila'
Primary publication:
Structural and mutagenetic analyses of a 1,3-1,4-β-glucanase from Paecilomyces thermophila.
Cheng YS, Huang CH, Chen CC, Huang TY, Ko TP, Huang JW, Wu TH, Liu JR, Guo RT
Biochim Biophys Acta 1844 366-73 (2014)
PMID: 24262091

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122728 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH16 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 298 amino acids
Theoretical weight: 32.22 KDa
Source organism: Paecilomyces sp. 'thermophila'
Expression system: Komagataella pastoris
UniProt:
  • Canonical: E0XN39 (Residues: 19-314; Coverage: 100%)
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: C2221
Unit cell:
a: 88.342Å b: 172.928Å c: 167.084Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.208
Expression system: Komagataella pastoris

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Citations

1 review citation

The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications.
Goldenkova-Pavlova et al. (2018)
7 other articles

3 mentions without citation

The agar-specific hydrolase ZgAgaC from the marine bacterium Zobellia galactanivorans defines a new GH16 protein subfamily.
Naretto et al. (2019)
2 more