Structure of PDB 4gyj Chain B Binding Site BS02

Receptor Information
>4gyj Chain B (length=617) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASASKRAIDANQIVNRMSLDEKLGQMLMPDFRNWQKEGESSPQALTKMND
EVASLVKKYQFGGIILFAENVKTTKQTVQLTDDYQKASPKIPLMLSIDQE
GGIVTRLGEGTNFPGNMALGAARSRINAYQTGSIIGKELSALGINTDFSP
VVDINNNPDNPVIGVRSFSSNRELTSRLGLYTMKGLQRQDIASALKHFPG
HGDTDVDSHYGLPLVSHGQERLREVELYPFQKAIDAGADMVMTAHVQFPA
FDDTTYKSKLDGSDILVPATLSKKVMTGLLRQEMGFNGVIVTNALNMKAI
ADHFGQEEAVVMAVKAGVDIALMPASVTSLKEEQKFARVIQALKEAVKNG
DIPEQQINNSVERIISLKIKRGMYPARNSDSTKEKIAKAKKIVGSKQHLK
AEKKLAEKAVTVLKNEQHTLPFKPKKGSRILIVAPYEEQTASIEQTIHDL
IKRKKIKPVSLSKMNFASQVFKTEHEKQVKEADYIITGSYVVKNDPVVND
GVIDDTISDSSKWATVFPRAVMKAALQHNKPFVLMSLRNPYDAANFEEAK
ALIAVYGFKGYANGRYLQPNIPAGVMAIFGQAKPKGTLPVDIPSVTKPGN
TLYPLGYGLNIKTGRPL
Ligand information
Ligand IDMUB
InChIInChI=1S/C11H19NO8/c1-4(10(16)17)19-9-7(12-5(2)14)11(18)20-6(3-13)8(9)15/h4,6-9,11,13,15,18H,3H2,1-2H3,(H,12,14)(H,16,17)/t4-,6-,7-,8-,9-,11+/m1/s1
InChIKeyMNLRQHMNZILYPY-MDMHTWEWSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[CH](O[CH]1[CH](O)[CH](CO)O[CH](O)[CH]1NC(C)=O)C(O)=O
ACDLabs 10.04O=C(O)C(OC1C(O)C(OC(O)C1NC(=O)C)CO)C
OpenEye OEToolkits 1.5.0CC(C(=O)O)OC1C(C(OC(C1O)CO)O)NC(=O)C
CACTVS 3.341C[C@@H](O[C@H]1[C@H](O)[C@@H](CO)O[C@H](O)[C@@H]1NC(C)=O)C(O)=O
OpenEye OEToolkits 1.5.0C[C@H](C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]1O)CO)O)NC(=O)C
FormulaC11 H19 N O8
NameN-acetyl-alpha-muramic acid;
N-acetyl-muramic acid;
N-ACETYLMURAMIC ACID
ChEMBLCHEMBL1234516
DrugBank
ZINCZINC000003861769
PDB chain4gyj Chain D Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4gyj Active Site Plasticity within the Glycoside Hydrolase NagZ Underlies a Dynamic Mechanism of Substrate Distortion.
Resolution1.65 Å
Binding residue
(original residue number in PDB)		R57 F92 R131 H234 N321 M322
Binding residue
(residue number reindexed from 1)		R32 F67 R106 H209 N296 M297
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N318 N524
Catalytic site (residue number reindexed from 1) N293 N499
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0009254 peptidoglycan turnover
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4gyj, PDBe:4gyj, PDBj:4gyj
PDBsum4gyj
PubMed23177201
UniProtP40406|NAGZ_BACSU Beta-hexosaminidase (Gene Name=nagZ)

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