Structure of PDB 6pa3 Chain D

Receptor sequence

>6pa3D (length=332) Species: 83333 (Escherichia coli K-12)

HHHHHHLPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKD
IANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGVDTMEE
TAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANR
GVLVVMNDTVLDGRDVTTTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPA
RKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGV
GNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVAS
GTLNPQKARVLLQLALTQTKDPQQIQQIFNQY

3D structure

• PDB: 6pa3 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
• Chain: D
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T12 Y25 V89 D90 T162 E283
• Catalytic site (residue number reindexed from 1): T18 Y31 V95 D96 T168 E289
• 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	D	T12 G57 S58 Q59 G88 V89 D90 A114	T18 G63 S64 Q65 G94 V95 D96 A120

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

External links

• PDB: RCSB:6pa3, PDBe:6pa3, PDBj:6pa3
• PDBsum: 6pa3
• PubMed: 31423681
• UniProt: P00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)