Structure of PDB 1ib4 Chain B

Receptor sequence

>1ib4B (length=339) Species: 5053 (Aspergillus aculeatus)

ATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVI
FSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGG
KTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDG
DDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSG
GHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVT
YKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGT
NILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC

3D structure

• PDB: 1ib4 The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex.
• Chain: B
• Resolution: 2.0 Å

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	B	T3 T5	T3 T5
BS02	MAN	B	S13 K17	S13 K17
BS03	MAN	B	N10 S14	N10 S14
BS04	MAN	B	K17 S18	K17 S18
BS05	MAN	B	A1 S23 G46	A1 S23 G46

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

External links

• PDB: RCSB:1ib4, PDBe:1ib4, PDBj:1ib4
• PDBsum: 1ib4
• PubMed: 11518536
• UniProt: O74213|PGLR1_ASPAC Endopolygalacturonase I (Gene Name=pgaI)