Structure of PDB 4uui Chain D

Receptor sequence
>4uuiD (length=299) Species: 562 (Escherichia coli) [Search protein sequence]
HHHATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGST
GEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRY
GFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVFNIPALSGVKLT
LDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDNIFASGL
LAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIK
TGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG
3D structure
PDB4uui A Case Study for Twinned Data Analysis: Multiple Crystal Forms of the Enzyme N-Acetyl-Neuraminic Lyase
ChainD
Resolution1.79 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 F137 L142 K165 I206
Catalytic site (residue number reindexed from 1) S49 Y112 F139 L144 K167 I208
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 D191 N192 D193 N194
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:4uui, PDBe:4uui, PDBj:4uui
PDBsum4uui
PubMed
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

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