Structure of PDB 6nxc Chain A

Receptor sequence
>6nxcA (length=326) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KKSIYVAYTGGTIGMQRSIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTP
LMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLE
NLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLY
RGNRTAKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHP
ITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQE
LQEASDRGIVVVNLTQCMSGKVNMGNALAHAGVIGGADMTVEATLTKLHY
LLSQELDTETIRKAMSQNLRGELTPD
3D structure
PDB6nxc Opportunistic complexes of E. coli L-asparaginases with citrate anions.
ChainA
Resolution1.74 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 G286
Catalytic site (residue number reindexed from 1) T12 T85 D86 K157 G275
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 A R240 C273 T301 V302 E303 R234 C267 T290 V291 E292
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:6nxc, PDBe:6nxc, PDBj:6nxc
PDBsum6nxc
PubMed31363102
UniProtP0A962|ASPG1_ECOLI L-asparaginase 1 (Gene Name=ansA)

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