Structure of PDB 6pa2 Chain A

Receptor sequence
>6pa2A (length=313) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
HLPNITILATGGTIAGVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMND
NVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVG
AMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTMT
NTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPK
VGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKT
GTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQT
KDPQQIQQIFNQY
3D structure
PDB6pa2 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
ChainA
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) T12 T89 D90 M162 E283
Catalytic site (residue number reindexed from 1) T13 T76 D77 M149 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 ASP A T12 G57 S58 Q59 G88 T89 D90 A114 T13 G44 S45 Q46 G75 T76 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:6pa2, PDBe:6pa2, PDBj:6pa2
PDBsum6pa2
PubMed31423681
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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