Structure of PDB 5gqb Chain A

Receptor sequence
>5gqbA (length=538) Species: 93504 (Ostrinia furnacalis) [Search protein sequence]
AAAPPGKPSLGWGERTFAIVEVNQAATAYNQLVTKRDSADVSVTWNVWSG
DPADKARVLLNDKEFWSGTGGAAGSASFKVKKGGRYQMVVELCNADGCSQ
SDATEIIVADTDGSHLPPLDYNMGEKNKPFKQTSGKVVGAYFVEWGVYPR
KFPVDRVPIPNLTHLLYGFIPICGGDGINDSLKEIEGSFQALQRSCSGRE
DFKVSIHDPWAALQKPQKGLSSWNEPYKGNFGQLMMLKQAKPDLKILPSI
GGWTLADPFFFFTDETKRRRFVASVKDFLQTWKFFDGVDIDWEFPGGKGA
NPNLGSPKDGEIYVLLMKELREMLNELSAETGRKYELTSAISAGWDKIQV
VDYSAAQKYMDHIFFMSYDFKGAWSNDTLGHQASLYAPDWNEKETYTTDF
GVQFLLAQGVSPKKIVVGVAMYGRGWTGVHGYKDNNPFTGNATGPVKGTW
QDGVVDYREIATEIAQGKWEYHYDKVAQAPYVFRPATGDLITYDDARSTI
EKGKYVRANKLGGLFAWEIDADNGDILNAMNMGLGNSA
3D structure
PDB5gqb Structure, Catalysis, and Inhibition of OfChi-h, the Lepidoptera-exclusive Insect Chitinase.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D304 D306 E308 Y383
Catalytic site (residue number reindexed from 1) D289 D291 E293 Y368
Enzyme Commision number ?
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 W268 D384 W253 D369
BS02 GCS A G267 W268 E308 W532 G252 W253 E293 W517
BS03 GCS A F184 W268 T269 L270 F169 W253 T254 L255
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004568 chitinase activity
GO:0008061 chitin binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006032 chitin catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5gqb, PDBe:5gqb, PDBj:5gqb
PDBsum5gqb
PubMed28053084
UniProtQ4AE59

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