Structure of PDB 4bwl Chain D

Receptor sequence
>4bwlD (length=298) Species: 562 (Escherichia coli) [Search protein sequence]
HHHHATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGS
TGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKR
YGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVANIPALSGVKL
TLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASG
LLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLI
KTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQE
3D structure
PDB4bwl The Reaction Mechanism of N-Acetylneuraminic Acid Lyase Revealed by a Combination of Crystallography, Qm/Mm Simulation and Mutagenesis.
ChainD
Resolution2.0 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 A137 L142 K165 I206
Catalytic site (residue number reindexed from 1) S50 Y113 A140 L145 K168 I209
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 SI3 D S47 T48 K165 T167 G189 Y190 D191 E192 G207 S208 F252 S50 T51 K168 T170 G192 Y193 D194 E195 G210 S211 F255
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:4bwl, PDBe:4bwl, PDBj:4bwl
PDBsum4bwl
PubMed24521460
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

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