Structure of PDB 1f74 Chain A

Receptor sequence
>1f74A (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.
ChainA
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 Y136 L141 K164 I205
Catalytic site (residue number reindexed from 1) S47 Y110 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 NAY A A10 S47 T48 K164 F189 D190 E191 G206 S207 A10 S47 T48 K164 F189 D190 E191 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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