Structure of PDB 2p2n Chain B

Receptor sequence
>2p2nB (length=321) Species: 562 (Escherichia coli) [Search protein sequence]
PRGSHMQKKSIYVAYTGGSGHLQRQLALMPEFHRPEMPDFTIHEYTPLMD
SSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLG
KPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGN
RTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITP
QPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQE
ASDRGIVVVNLTQCMSGKVNMALAHAGVIGGADMTVEATLTKLHYLLSQE
LDTETIRKAMSQNLRGELTPD
3D structure
PDB2p2n Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia colil-Asparaginase I
ChainB
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) T82 D83 K154
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 B D59 S60 G90 T91 D92 D50 S51 G81 T82 D83
BS02 ASN B D59 S60 S61 G90 D92 D50 S51 S52 G81 D83
BS03 ASN B T162 R240 Q272 C273 T301 V302 E303 T153 R231 Q263 C264 T285 V286 E287
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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