BioLiP

Structure of PDB 1fdz Chain D

Receptor sequence

>1fdzD (length=292) Species: 562 (Escherichia coli) [Search protein sequence]

NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFV
QSLSEREQVLEIVAEEGKGKIKLIAHVGCVTTAESQQLAASAKRYGFDAV
SAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQIN
TLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGAD
GGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFR
GLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQE

3D structure

PDB

1fdz Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.

Chain

Resolution

2.6 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 Y137 L142 K165 I206
Catalytic site (residue number reindexed from 1)	S44 Y107 Y134 L139 K162 I203
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	PYR	D	Y43 S47 T48 Y137 K165	Y40 S44 T45 Y134 K162

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

PDB	RCSB:1fdz, PDBe:1fdz, PDBj:1fdz
PDBsum	1fdz
PubMed	9047371
UniProt	P0A6L4\|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)