BioLiP

Structure of PDB 3wqv Chain A

Receptor sequence

>3wqvA (length=383) Species: 93504 (Ostrinia furnacalis) [Search protein sequence]

RARVVCYFSNWAVYRPGVGRYGIEDIPVDMCTHIIYSFIGVTEDTQQVLI
IDPELDVDKNGFKNFTSLRSKHPGVKFTVAVGGWAEGGSKYSKMVAAKST
RMAFVRSVVDFLNKYNFDGLDLDWEYPGAADRGGSFSDKDKFLYLVQELR
RAFIREGKGWELTAAVPLANFRLMEGYHVPELCQELDAIHVMSYDLRGNW
AGFADVHSPLYKRPHDQWAYEKLNVNDGLQLWEDKGCPTNKLVVGIPFYG
RSFTLSSGNNNYNLGTYINKEAGGGDPAPYTNATGFWAYYEICTEVDTAD
SKWTKKWDEHGKCPYAYKGTQWVGYEDPRSVEIKMNWIKEKGYLGAMTWA
IDMDDFQGLCGEKNILIKLLHKHMSAYTVPPPR

3D structure

PDB

3wqv Fully deacetylated chitooligosaccharides act as efficient glycoside hydrolase family 18 chitinase inhibitors.

Chain

Resolution

2.043 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D144 D146 E148 Y217
Catalytic site (residue number reindexed from 1)	D121 D123 E125 Y194
Enzyme Commision number	3.2.1.14: chitinase.

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	GCS	A	F61 W107 D146 E148 M215 Y217 D218 W372	F38 W84 D123 E125 M192 Y194 D195 W349	PDBbind-CN: -logKd/Ki=5.21,Kd=6.2uM
BS02	GCS	A	F61 G106 A108	F38 G83 A85	PDBbind-CN: -logKd/Ki=5.21,Kd=6.2uM

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008061	chitin binding

	Biological Process
GO:0005975	carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:3wqv, PDBe:3wqv, PDBj:3wqv
PDBsum	3wqv
PubMed	24828498
UniProt	Q2V6H4