Structure of PDB 6pa3 Chain A

Receptor sequence
>6pa3A (length=334) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MDHHHHHHLPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQL
KDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGVDTM
EETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASA
NRGVLVVMNDTVLDGRDVTTTNTTDVATFKSVNYGPLGYIHNGKIDYQRT
PARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSA
GVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFV
ASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY
3D structure
PDB6pa3 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
ChainA
Resolution1.65 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 V89 D90 T162 E283
Catalytic site (residue number reindexed from 1) T20 Y33 V97 D98 T170 E291
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 A T12 G57 S58 Q59 G88 V89 D90 T20 G65 S66 Q67 G96 V97 D98
BS02 MG A H-4 H-2 H4 H6
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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Cellular Component
External links
PDB RCSB:6pa3, PDBe:6pa3, PDBj:6pa3
PDBsum6pa3
PubMed31423681
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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