Structure of PDB 2p2n Chain D

Receptor sequence
>2p2nD (length=319) Species: 562 (Escherichia coli) [Search protein sequence]
VPRGSHMQKKSIYVAYTGGHLQRQLALMPEFHRPEMPDFTIHEYTPLMDS
SDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLGK
PVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNR
TTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQ
PIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQEA
SDRGIVVVNLTQCMSGKVNALAHAGVIGGADMTVEATLTKLHYLLSQELD
TETIRKAMSQNLRGELTPD
3D structure
PDB2p2n Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia colil-Asparaginase I
ChainD
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) T91 D92 K163
Catalytic site (residue number reindexed from 1) T81 D82 K153
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 D D59 S60 G90 T91 D92 D49 S50 G80 T81 D82
BS02 ASN D D59 S60 S61 G90 D92 D49 S50 S51 G80 D82
BS03 ASN D T162 R240 Q272 C273 T301 V302 E303 T152 R230 Q262 C263 T283 V284 E285
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:0033345 asparagine catabolic process via L-aspartate
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2p2n, PDBe:2p2n, PDBj:2p2n
PDBsum2p2n
PubMed17451745
UniProtP0A962|ASPG1_ECOLI L-asparaginase 1 (Gene Name=ansA)

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