Structure of PDB 3s6t Chain A

Receptor sequence
>3s6tA (length=575) Species: 93504 (Ostrinia furnacalis) [Search protein sequence]
VAAEDVVWRWSCDNGKCVKLKNDPRSSEPALSLEACKMFCNEYGLLWPRP
TGEADLGNFLSKINLNSIEVKILKKGATDDLMEAAAKRFKEQVSLAIPRG
STPKLTGKAVDVYLVNENPNEKAFSLEMDESYGLRVSPSGADRVNATITA
NSFFGMRHGLETLSQLFVFDDIRDHLLMVRDVNISDKPVYPYRGILLDTA
RNYYSIESIKRTIEAMAAVKLNTFHWHITDSQSFPFVTTKRPNLYKFGAL
SPQKVYTKAAIREVVRFGLERGVRVLPEFDAPAHVGEGWQDTDLTVCFKA
EPWKSYCGEPPCGQLNPTKDELYQYLEDIYSDMAEVFDTTDIFHMGGDEV
SEACWNSSDSIQNFMMQNRWDLDKESFLKLWNYFQQKAQDKAYKAFGKKL
PLILWTSTLTNYKHIDDYLNKDDYIIQVWTTGVDPQIKGLLEKGYRLIMS
NYDALYFDCGYGAWVGAGNNWCSPYIGWQKVYDNSPAVIALEHRDQVLGG
EAALWSEQSDTSTLDGRLWPRAAALAERLWAEPATSWQDAEYRMLHIRER
LVRMGIQAESLQPEWCYQNEGYCYS
3D structure
PDB3s6t Active-pocket size differentiating insectile from bacterial chitinolytic beta-N-acetyl-D-hexosaminidases.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D367 E368
Catalytic site (residue number reindexed from 1) D348 E349
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 OAN A R220 D367 W424 W448 Y475 D477 W490 W524 E526 R201 D348 W405 W429 Y456 D458 W471 W505 E507 MOAD: Ki=0.045uM
PDBbind-CN: -logKd/Ki=7.35,Ki=45nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3s6t, PDBe:3s6t, PDBj:3s6t
PDBsum3s6t
PubMed21692744
UniProtQ06GJ0|HEXC_OSTFU Chitooligosaccharidolytic beta-N-acetylglucosaminidase

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