Structure of PDB 3eca Chain A

Receptor sequence
>3ecaA (length=326) Species: 562 (Escherichia coli) [Search protein sequence]
LPNITILATGGTIAGGGDSATKSNYTAGKVGVENLVNAVPQLKDIANVKG
EQVVNIGSQDMNDDVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD
LTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVM
NDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSD
TPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLY
KTVFDTLATAAKNGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQ
KARVLLQLALTQTKDPQQIQQIFNQY
3D structure
PDB3eca Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T12 Y25 T89 D90 K162 E283
Catalytic site (residue number reindexed from 1) T12 Y25 T89 D90 K162 E283
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 A T12 G57 S58 Q59 G88 T89 D90 T12 G57 S58 Q59 G88 T89 D90
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006528 asparagine metabolic process
GO:0006530 asparagine catabolic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0032991 protein-containing complex
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3eca, PDBe:3eca, PDBj:3eca
PDBsum3eca
PubMed8434007
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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