Structure of PDB 6nxd Chain B

Receptor sequence
>6nxdB (length=325) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PRGSHMQKKSIYVAYTGGTIGMSGHLQRQLALMPEFHRPEMPDFTIHEYT
PLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFML
ENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRL
YRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVH
PITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQ
ELQEASDRGIVVVNLTQCMSGKVNMALAHAGVIGGADMTVEATLTKLHYL
LSQELDTETIRKAMSQNLRGELTPD
3D structure
PDB6nxd Opportunistic complexes of E. coli L-asparaginases with citrate anions.
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) T14 T91 D92 K163
Catalytic site (residue number reindexed from 1) T19 T86 D87 K158
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 B T162 R240 Q272 C273 T301 V302 E303 T157 R235 Q267 C268 T289 V290 E291
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:6nxd, PDBe:6nxd, PDBj:6nxd
PDBsum6nxd
PubMed31363102
UniProtP0A962|ASPG1_ECOLI L-asparaginase 1 (Gene Name=ansA)

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