Structure of PDB 3lbc Chain D

Receptor sequence
>3lbcD (length=296) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGE
AFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGF
DAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLD
QINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLA
GADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTG
VFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQER
3D structure
PDB3lbc Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val251
ChainD
Resolution1.85 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) S47 Y110 Y137 L142 K165 I206
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 LAI D D170 Y172 D170 Y172
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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Cellular Component
External links
PDB RCSB:3lbc, PDBe:3lbc, PDBj:3lbc
PDBsum3lbc
PubMed
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

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