Structure of PDB 2hln Chain B

Receptor sequence
>2hlnB (length=308) Species: 29471 (Pectobacterium atrosepticum) [Search protein sequence]
NLPNIVILATGGTIAGVETLIQAVPELKTLANIKGEQVASIGSENMTSDV
LLTLSKRVNELLARSDVDGVVITHGTDTLDESPYFLNLTVKSDKPVVFVA
AMRPATAISADGPMNLYGAVKVAADKNSRGRGVLVVLNDRIGSARFISKT
NASTLDTFKAPEEGYLGVIIGDKIYYQTRLDKVHTTRSVFDVTNVDKLPA
VDIIYGYQDDPEYMYDASIKHGVKGIVYAGMGAGSVSKRGDAGIRKAESK
GIVVVRSSRTGSGIVPPDAGQPGLVADSLSPAKSRILLMLALTKTTNPAV
IQDYFHAY
3D structure
PDB2hln Three-dimensional structures of L-asparaginase from Erwinia carotovora complexed with aspartate and glutamate.
ChainB
Resolution2.2 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 T95 D96 K168
Catalytic site (residue number reindexed from 1) T13 T76 D77 K149
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 GLU B G14 T15 G61 S62 E63 G94 T95 D96 A120 G12 T13 G42 S43 E44 G75 T76 D77 A101
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:2hln, PDBe:2hln, PDBj:2hln
PDBsum2hln
PubMed18323619
UniProtQ7WWK9

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