Structure of PDB 6pa6 Chain D

Receptor sequence
>6pa6D (length=314) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LPNITILATGGTIAGGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMN
DNVWLTLAKKINTDCDKTDGFVITHGVDTMEETAYFLDLTVKCDKPVVMV
GAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTT
TNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELP
KVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAK
TGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQ
TKDPQQIQQIFNQY
3D structure
PDB6pa6 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
ChainD
Resolution2.12 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 V77 D78 T150 E271
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 T12 G45 S46 Q47 G76 V77 D78
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:6pa6, PDBe:6pa6, PDBj:6pa6
PDBsum6pa6
PubMed31423681
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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