Structure of PDB 1hg0 Chain A

Receptor sequence
>1hg0A (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
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A T15 A61 S62 G94 T95 D96 T15 A61 S62 G94 T95 D96
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)

[Back to BioLiP]