Structure of PDB 2wpb Chain A

Receptor sequence
>2wpbA (length=302) Species: 562 (Escherichia coli) [Search protein sequence]
HHHHHHATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVG
GSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASA
KRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGV
KLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDNIFA
SGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDL
LIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQE
RG
3D structure
PDB2wpb Structural Insights Into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution.
ChainA
Resolution2.05 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) S52 Y115 Y142 L147 K170 I211
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 ZZI A G189 Y190 D191 N192 S208 G194 Y195 D196 N197 S213 MOAD: Ki=1.3mM
PDBbind-CN: -logKd/Ki=2.89,Ki=1.3mM
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:2wpb, PDBe:2wpb, PDBj:2wpb
PDBsum2wpb
PubMed20826162
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

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