Structure of PDB 1ia5 Chain A

Receptor sequence
>1ia5A (length=339) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
ATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVI
FSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGG
KTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDG
DDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSG
GHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVT
YKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGT
NILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC
3D structure
PDB1ia5 The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D159 D180 D181 H202 R235 K237
Catalytic site (residue number reindexed from 1) D159 D180 D181 H202 R235 K237
Enzyme Commision number 3.2.1.15: endo-polygalacturonase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MAN A N10 S13 N10 S13
BS02 MAN A A1 C22 S23 N44 A1 C22 S23 N44
BS03 MAN A S34 K60 S34 K60
Gene Ontology
Molecular Function
GO:0004650 polygalacturonase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045490 pectin catabolic process
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1ia5, PDBe:1ia5, PDBj:1ia5
PDBsum1ia5
PubMed11518536
UniProtO74213|PGLR1_ASPAC Endopolygalacturonase I (Gene Name=pgaI)

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