Structure of PDB 2him Chain B

Receptor sequence
>2himB (length=329) Species: 562 (Escherichia coli) [Search protein sequence]
VPRGSHMQKKSIYVAYTGGTIGMQRSGHLQRQLALMPEFHRPEMPDFTIH
EYTPLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALS
FMLENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFN
NRLYRGNRTAKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGEL
IVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKA
FLQELQEASDRGIVVVNLTQCMSGKVNMNALAHAGVIGGADMTVEATLTK
LHYLLSQELDTETIRKAMSQNLRGELTPD
3D structure
PDB2him Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I.
ChainB
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 T89 D90 K161
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 T14 D59 S60 G90 T91 D92 T20 D57 S58 G88 T89 D90
BS02 ASN B R240 Q272 C273 T301 V302 E303 R238 Q270 C271 T293 V294 E295
BS03 ASN B T14 D59 S60 S61 G90 D92 T20 D57 S58 S59 G88 D90
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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