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Structure of PDB 2gvn Chain D

Receptor sequence
>2gvnD (length=325) Species: 29471 (Pectobacterium atrosepticum) [Search protein sequence]
NLPNIVILATGGTIAGSAAANTQTTGYKAGALGVETLIQAVPELKTLANI
KGEQVASIGSENMTSDVLLTLSKRVNELLARSDVDGVVITHGTDTLDESP
YFLNLTVKSDKPVVFVAAMRPATAISADGPMNLYGAVKVAADKNSRGRGV
LVVLNDRIGSARFISKTNASTLDTFKAPEEGYLGVIIGDKIYYQTRLDKV
HTTRSVFDVTNVDKLPAVDIIYGYQDDPEYMYDASIKHGVKGIVYAGMGA
GSVSKRGDAGIRKAESKGIVVVRSSRTGSGIVPPDAGQPGLVADSLSPAK
SRILLMLALTKTTNPAVIQDYFHAY
3D structure
PDB2gvn Three-dimensional structures of L-asparaginase from Erwinia carotovora complexed with aspartate and glutamate.
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) T13 Y27 T93 D94 K166
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 ASP D T15 G61 S62 E63 G94 T95 D96 T13 G59 S60 E61 G92 T93 D94
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

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