Structure of PDB 2him Chain D

Receptor sequence
>2himD (length=331) Species: 562 (Escherichia coli) [Search protein sequence]
VPRGSHMQKKSIYVAYTGGTIGMQRIPVSGHLQRQLALMPEFHRPEMPDF
TIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTAS
ALSFMLENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTL
FFNNRLYRGNRTAKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE
GELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQ
NKAFLQELQEASDRGIVVVNLTQCMSGKVNMALAHAGVIGGADMTVEATL
TKLHYLLSQELDTETIRKAMSQNLRGELTPD
3D structure
PDB2him Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I.
ChainD
Resolution1.82 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T14 T91 D92 K163
Catalytic site (residue number reindexed from 1) T20 T92 D93 K164
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 T14 D59 S60 G90 T91 D92 T20 D60 S61 G91 T92 D93
BS02 ASN D R240 Q272 C273 T301 V302 E303 R241 Q273 C274 T295 V296 E297
BS03 ASN D T14 D59 S60 S61 G90 D92 T20 D60 S61 S62 G91 D93
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:2him, PDBe:2him, PDBj:2him
PDBsum2him
PubMed17451745
UniProtP0A962|ASPG1_ECOLI L-asparaginase 1 (Gene Name=ansA)

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