Structure of PDB 1hl2 Chain A

Receptor sequence
>1hl2A (length=295) Species: 562 (Escherichia coli) [Search protein sequence]
TNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAF
VQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFDA
VSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPARSGVKLTLDQI
NTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGA
DGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVF
RGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG
3D structure
PDB1hl2 Mimicking Natural Evolution in Vitro: An N-Acetylneuraminate Lyase Mutant with an Increased Dihydrodipicolinate Synthase Activity
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S47 Y110 Y137 R142 K165 I206
Catalytic site (residue number reindexed from 1) S45 Y108 Y135 R140 K163 I204
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 3PY A Y43 G46 S47 T48 Y137 K165 Y41 G44 S45 T46 Y135 K163
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hl2, PDBe:1hl2, PDBj:1hl2
PDBsum1hl2
PubMed12711733
UniProtP0A6L4|NANA_ECOLI N-acetylneuraminate lyase (Gene Name=nanA)

[Back to BioLiP]