Structure of PDB 1f74 Chain C

Receptor sequence
>1f74C (length=293) Species: 727 (Haemophilus influenzae) [Search protein sequence]
MRDLKGIFSALLVSFNEDGTINEKGLRQIIRHNIDKMKVDGLYVGGSTGE
NFMLSTEEKKEIFRIAKDEAKDQIALIAQVGSVNLKEAVELGKYATELGY
DCLSAVTPFYYKFSFPEIKHYYDTIIAETGSNMIVYSIPFLTGVNMGIEQ
FGELYKNPKVLGVKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLG
VDGAIGSTFNVNGVRARQIFELTKAGKLKEALEIQHVTNDLIEGILANGL
YLTIKELLKLEGVDAGYCREPMTSKATAEQVAKAKDLKAKFLS
3D structure
PDB1f74 Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.
ChainC
Resolution1.6 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 L141
Catalytic site (residue number reindexed from 1) S47 Y110 L141
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 NAY C A10 S47 T48 K164 G188 F189 D190 E191 I205 G206 S207 A10 S47 T48 K164 G188 F189 D190 E191 I205 G206 S207 MOAD: Ki=0.9mM
PDBbind-CN: -logKd/Ki=3.05,Ki=0.9mM
Gene Ontology
Molecular Function
GO:0008747 N-acetylneuraminate lyase activity
GO:0016829 lyase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0019262 N-acetylneuraminate catabolic process
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:1f74, PDBe:1f74, PDBj:1f74
PDBsum1f74
PubMed11031117
UniProtP44539|NANA_HAEIN N-acetylneuraminate lyase (Gene Name=nanA)

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