Structure of PDB 1ib4 Chain A

Receptor sequence
>1ib4A (length=339) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
ATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVI
FSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGG
KTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDG
DDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSG
GHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVT
YKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGT
NILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC
3D structure
PDB1ib4 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 S13 K17 S13 K17
BS02 MAN A N10 S14 N10 S14
BS03 MAN A S21 S23 N44 S21 S23 N44
BS04 MAN A T24 H48 T24 H48
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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Biological Process
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Cellular Component
External links
PDB RCSB:1ib4, PDBe:1ib4, PDBj:1ib4
PDBsum1ib4
PubMed11518536
UniProtO74213|PGLR1_ASPAC Endopolygalacturonase I (Gene Name=pgaI)

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