› 4asl

X-ray diffraction
1.24Å resolution

Structure of Epa1A in complex with the T-antigen (Gal-b1-3- GalNAc)

Released:
DOI: 10.2210/pdb4asl/pdb
Model geometry
Fit model/data
PDB entry 4asl coloured by chain, front view.
PDB entry 4asl coloured by chain, side view.
PDB entry 4asl coloured by chain, top view.
Source organism: [Candida] glabrata
Primary publication:
Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.
Maestre-Reyna M, Diderrich R, Veelders MS, Eulenburg G, Kalugin V, Brückner S, Keller P, Rupp S, Mösch HU, Essen LO
Proc Natl Acad Sci U S A 109 16864-9 (2012)
PMID: 23035251

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179632 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
PA14 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.16 KDa
Source organism: [Candida] glabrata
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6FUW5 (Residues: 31-271; Coverage: 24%)
Gene names: CAGL0E06644g, EPA1
Sequence domains: GLEYA domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NGA, GAL
Carbohydrate polymer
3 bound ligands:
Ligand CA 1 x CA
Ligand NA 5 x NA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 74.6Å b: 103.9Å c: 69.4Å
α: 89.9° β: 90° γ: 89.9°
R-values:
R R work R free
0.119 0.117 0.155
Expression system: Escherichia coli BL21

Quick links

Citations

14 review citations

Adhesins in human fungal pathogens: glue with plenty of stick.
de Groot et al. (2013)
13 more

9 mentions without citation

Adhesins of Yeasts: Protein Structure and Interactions.
Willaert RG. (2018)
8 more