Structure of PDB 6pa5 Chain E

Receptor sequence
>6pa5E (length=313) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LPNITILATGGTIAGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMND
NVWLTLAKKINTDCDKTDGFVITHGVDTMEETAYFLDLTVKCDKPVVMVG
AMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTTT
NTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPK
VGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKT
GTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQT
KDPQQIQQIFNQY
3D structure
PDB6pa5 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
ChainE
Resolution2.0 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 V89 D90 T162 E283
Catalytic site (residue number reindexed from 1) T12 V76 D77 T149 E270
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 ASN E T12 G57 S58 Q59 G88 V89 D90 A114 T12 G44 S45 Q46 G75 V76 D77 A101
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:6pa5, PDBe:6pa5, PDBj:6pa5
PDBsum6pa5
PubMed31423681
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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