Structure of PDB 3ljq Chain C

Receptor sequence
>3ljqC (length=288) Species: 238 (Elizabethkingia meningoseptica) [Search protein sequence]
SEPSTTNKPIVLSTWNFGLHANVEAWKVLSKGGKALDAVEKGVRLVEDDP
TERSVGYGGRPDRDGRVTLDACIMDENYNIGSVACMEHIKNPISVARAVM
EKTPHVMLVGDGALEFALSQGFKKENLLTAESEKEWKEWLKNHDCIGMIA
LDAQGNLSGACTTSGMAYKMHGRVGDSPIIGAGLFVDNEIGAATATGHGE
EVIRTVGTHLVVELMNQGRTPQQACKEAVERIVKIVNRRGKNLKDIQVGF
IALNKKGEYGAYCIQDGFNFAVHDQKGNRLETPGFALK
3D structure
PDB3ljq Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing.
ChainC
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) C452
Catalytic site (residue number reindexed from 1) C145
Enzyme Commision number 3.5.1.26: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase.
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 GLY C D451 R480 D483 G504 G506 D144 R173 D176 G197 G199
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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