Structure of PDB 3ljq Chain C Binding Site BS01

Receptor Information
>3ljq Chain C (length=288) Species: 238 (Elizabethkingia meningoseptica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEPSTTNKPIVLSTWNFGLHANVEAWKVLSKGGKALDAVEKGVRLVEDDP
TERSVGYGGRPDRDGRVTLDACIMDENYNIGSVACMEHIKNPISVARAVM
EKTPHVMLVGDGALEFALSQGFKKENLLTAESEKEWKEWLKNHDCIGMIA
LDAQGNLSGACTTSGMAYKMHGRVGDSPIIGAGLFVDNEIGAATATGHGE
EVIRTVGTHLVVELMNQGRTPQQACKEAVERIVKIVNRRGKNLKDIQVGF
IALNKKGEYGAYCIQDGFNFAVHDQKGNRLETPGFALK
Ligand information
Ligand IDGLY
InChIInChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
InChIKeyDHMQDGOQFOQNFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(=O)O)N
CACTVS 3.341NCC(O)=O
ACDLabs 10.04O=C(O)CN
FormulaC2 H5 N O2
NameGLYCINE
ChEMBLCHEMBL773
DrugBankDB00145
ZINCZINC000004658552
PDB chain3ljq Chain C Residue 596 [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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PDB3ljq Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D451 R480 D483 G504 G506
Binding residue
(residue number reindexed from 1)		D144 R173 D176 G197 G199
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C452
Catalytic site (residue number reindexed from 1) C145
Enzyme Commision number 3.5.1.26: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase.
Gene Ontology
Molecular Function
GO:0003948 N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
GO:0004067 asparaginase activity
GO:0008233 peptidase activity
GO:0008798 beta-aspartyl-peptidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0006517 protein deglycosylation
Cellular Component
GO:0005737 cytoplasm
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ljq, PDBe:3ljq, PDBj:3ljq
PDBsum3ljq
PubMed20800597
UniProtQ47898|ASPG_ELIMR N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

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