Structure of PDB 3suw Chain A

Receptor sequence
>3suwA (length=504) Species: 192895 (Paenibacillus sp. TS12) [Search protein sequence]
HHHHSSGLVPRGSHMSQPSILPKPVSYTVGSGQFVLTKNASIFVAGNNVG
ETDELFNIGQALAKKLNASTGYTISVVKSNQPTAGSIYLTTVGGNAALGN
EGYDLITTSNQVTLTANKPEGVFRGNQTLLQLLPAGIEKNTVVSGVQWVI
PHSNISDKPEYEYRGLMLDVARHFFTVDEVKRQIDLASQYKINKFHMHLS
DDQGWRIEIKSWPDLIEIGSKGQVGGGPGGYYTQEQFKDIVSYAAERYIE
VIPEIDMPGHTNAALASYGELNPDGKRKAMRTDTAVGYSTLMPRAEITYQ
FVEDVISELAAISPSPYIHLGGDESNATSAADYDYFFGRVTAIANSYGKK
VVGWDPSDTSSGATSDSVLQNWTCSASTGTAAKAKGMKVIVSPANAYLDM
KYYSDSPIGLQWRGFVNTNRAYNWDPTDCIKGANIYGVESTLWTETFVTQ
DHLDYMLYPKLLSNAEVGWTARGDRNWDDFKERLIEHTPRLQNKGIKFFA
DPIV
3D structure
PDB3suw Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L19 Y25 D321 E322
Catalytic site (residue number reindexed from 1) L21 Y27 D323 E324
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 GC2 A R170 D321 E322 W352 W370 Y395 W410 W441 E443 R172 D323 E324 W354 W372 Y397 W412 W443 E445 MOAD: Ki=20uM
PDBbind-CN: -logKd/Ki=4.70,Ki=20uM
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:3suw, PDBe:3suw, PDBj:3suw
PDBsum3suw
PubMed22367352
UniProtD2KW09

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