Structure of PDB 6nxd Chain C

Receptor sequence
>6nxdC (length=311) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KKSIYVAYTGGTIGMQLALMPEFHRPEMPDFTIHEYTPLMDSSDMTPEDW
QHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQ
IPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTKAHADG
FDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIY
PGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQEASDRGIVVV
NLTQCMSGKVNMALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKA
MSQNLRGELTP
3D structure
PDB6nxd Opportunistic complexes of E. coli L-asparaginases with citrate anions.
ChainC
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) T12 T73 D74 K145
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 C T162 R240 Q272 C273 T301 V302 E303 T144 R222 Q254 C255 T276 V277 E278
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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