Structure of PDB 2wpb Chain B

Receptor sequence
>2wpbB (length=295) Species: 562 (Escherichia coli) [Search protein sequence]
ATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEA
FVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFD
AVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQ
INTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDNIFASGLLAG
ADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGV
FRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQER
3D structure
PDB2wpb Structural Insights Into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution.
ChainB
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S47 Y110 Y137 L142 K165 I206
Catalytic site (residue number reindexed from 1) S46 Y109 Y136 L141 K164 I205
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 B G189 Y190 D191 G207 S208 G188 Y189 D190 G206 S207 MOAD: 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2wpb, PDBe:2wpb, PDBj:2wpb
PDBsum2wpb
PubMed20826162
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

[Back to BioLiP]