Structure of PDB 3bmx Chain A

Receptor sequence
>3bmxA (length=617) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ASASKRAIDANQIVNRMSLDEKLGQMLMPDFRNWQKEGESSPQALTKMND
EVASLVKKYQFGGIILFAENVKTTKQTVQLTDDYQKASPKIPLMLSIDQE
GGIVTRLGEGTNFPGNMALGAARSRINAYQTGSIIGKELSALGINTDFSP
VVDINNNPDNPVIGVRSFSSNRELTSRLGLYTMKGLQRQDIASALKHFPG
HGDTDVDSHYGLPLVSHGQERLREVELYPFQKAIDAGADMVMTAHVQFPA
FDDTTYKSKLDGSDILVPATLSKKVMTGLLRQEMGFNGVIVTDALNMKAI
ADHFGQEEAVVMAVKAGVDIALMPASVTSLKEEQKFARVIQALKEAVKNG
DIPEQQINNSVERIISLKIKRGMYPARNSDSTKEKIAKAKKIVGSKQHLK
AEKKLAEKAVTVLKNEQHTLPFKPKKGSRILIVAPYEEQTASIEQTIHDL
IKRKKIKPVSLSKMNFASQVFKTEHEKQVKEADYIITGSYVVKNDPVVND
GVIDDTISDSSKWATVFPRAVMKAALQHNKPFVLMSLRNPYDAANFEEAK
ALIAVYGFKGYANGRYLQPNIPAGVMAIFGQAKPKGTLPVDIPSVTKPGN
TLYPLGYGLNIKTGRPL
3D structure
PDB3bmx Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D318 N524
Catalytic site (residue number reindexed from 1) D293 N499
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 NA A H226 S233 A269 H270 D318 H201 S208 A244 H245 D293
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3bmx, PDBe:3bmx, PDBj:3bmx
PDBsum3bmx
PubMed20826810
UniProtP40406|NAGZ_BACSU Beta-hexosaminidase (Gene Name=nagZ)

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