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Polygalacturonase from aspergillus aculeatus

Analyse Polygalacturonase from aspergillus aculeatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IA5
Type
protein
Length
339 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polygalacturonase
EC
3.2.1.15
Ligands
MAN, NAG

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolygalacturonase (EC 3.2.1.15)protein3396% helix, 52% strand—

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 11 copies · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 11 glycan, 4 disulfide (O-glycosylation, disulfide, N-glycosylation).

Compared structures

  • 1IA5 · Polygalacturonase from aspergillus aculeatus · the same entry in another collection · chain A against A, TM-score 1.00

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