Structure of PDB 3lcw Chain A

Receptor sequence
>3lcwA (length=291) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFV
QSLSERAQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRHGFDAV
SAVTPFYYPFSLEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLGQIY
TLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD
GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGIFR
GLKTVLHYMDVISVPLCRKPFGPVDEKCLPELKALAQQLMQ
3D structure
PDB3lcw Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val251
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S47 Y110 Y137 L142 K165 I206
Catalytic site (residue number reindexed from 1) S44 Y107 Y134 L139 K162 I203
Enzyme Commision number 4.1.3.3: N-acetylneuraminate lyase.
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 3PY A Y43 G46 S47 T48 Y137 K165 Y40 G43 S44 T45 Y134 K162
Gene Ontology
Molecular Function
GO:0008747 N-acetylneuraminate lyase activity
GO:0016829 lyase activity
GO:0042802 identical protein binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0019262 N-acetylneuraminate catabolic process
GO:0044010 single-species biofilm formation
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:3lcw, PDBe:3lcw, PDBj:3lcw
PDBsum3lcw
PubMed
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

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