Structure of PDB 1jsr Chain D

Receptor sequence
>1jsrD (length=324) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
LPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVK
GEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEESAY
FLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVM
VVINDRIGSARYITKTNASTLDTFRANEEGYLGVIIGNRIYYQNRIDKLH
TTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAG
SVSVRGIAGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNPAHA
RILLMLALTRTSDPKVIQEYFHTY
3D structure
PDB1jsr Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?
ChainD
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T15 Y29 T95 D96 K168
Catalytic site (residue number reindexed from 1) T12 Y26 T92 D93 K165
Enzyme Commision number 3.5.1.1: 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 LDO D T15 Y29 A61 S62 E63 G94 T95 D96 A120 M121 T12 Y26 A58 S59 E60 G91 T92 D93 A117 M118
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006528 asparagine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1jsr, PDBe:1jsr, PDBj:1jsr
PDBsum1jsr
PubMed11755201
UniProtP06608|ASPG_DICCH L-asparaginase (Gene Name=ansB)

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