Structure of PDB 6pab Chain A

Receptor sequence

>6pabA (length=330) Species: 83333 (Escherichia coli K-12)

HHHHLPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIA
NVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETA
YFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGV
LVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARK
HTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGN
GNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGT
LNPQKARVLLQLALTQTKDPQQIQQIFNQY

3D structure

• PDB: 6pab Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
• Chain: A
• Resolution: 1.73 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T12 Y25 T89 D90 K162 E283
• Catalytic site (residue number reindexed from 1): T16 Y29 T93 D94 K166 E287
• 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 V27 G57 S58 Q59 G88 T89 D90	T16 V31 G61 S62 Q63 G92 T93 D94

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