Structure of PDB 1hg0 Chain D

Receptor sequence
>1hg0D (length=327) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
ADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLA
NVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEE
SAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGR
GVMVVINDRIGSARYITKTNASTLDTFRANEEGYLGVIIGNRIYYQNRID
KLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGM
GAGSVSVRGIAGMRKALEKGVVVMRSTRTGNGIVPPDEELPGLVSDSLNP
AHARILLMLALTRTSDPKVIQEYFHTY
3D structure
PDB1hg0 Stuctural Basis for the Activity and Substrate Specificity of Erwinia Chrysanthemi L-Asparaginase
ChainD
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) T15 Y29 T95 D96 K168
Catalytic site (residue number reindexed from 1) T15 Y29 T95 D96 K168
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 SIN D T15 S62 G94 T95 D96 A120 T15 S62 G94 T95 D96 A120
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1hg0, PDBe:1hg0, PDBj:1hg0
PDBsum1hg0
PubMed11341830
UniProtP06608|ASPG_DICCH L-asparaginase (Gene Name=ansB)

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