Structure of PDB 1dzw Chain P Binding Site BS01
Receptor Information
>1dzw Chain P (length=206) Species:
562
(Escherichia coli) [
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MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKL
TESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTA
VSILNRSIPAIHYMIAAAGGNSIPCAPYATAGTRELSEHVALALKNRKAT
LLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIA
VVLEKF
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1dzw Chain P Residue 999 [
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Receptor-Ligand Complex Structure
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PDB
1dzw
Catalytic Action of Fuculose 1-Phosphate Aldolase (Class II) as Derived from Structure-Directed Mutagenesis
Resolution
2.17 Å
Binding residue
(original residue number in PDB)
E73 H92 H94 H155
Binding residue
(residue number reindexed from 1)
E73 H92 H94 H155
Annotation score
1
Enzymatic activity
Enzyme Commision number
4.1.2.17
: L-fuculose-phosphate aldolase.
Gene Ontology
Molecular Function
GO:0008270
zinc ion binding
GO:0008738
L-fuculose-phosphate aldolase activity
GO:0016829
lyase activity
GO:0016830
carbon-carbon lyase activity
GO:0016832
aldehyde-lyase activity
GO:0046872
metal ion binding
Biological Process
GO:0005996
monosaccharide metabolic process
GO:0006004
fucose metabolic process
GO:0019317
fucose catabolic process
GO:0019323
pentose catabolic process
GO:0019568
arabinose catabolic process
GO:0019571
D-arabinose catabolic process
GO:0042355
L-fucose catabolic process
Cellular Component
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:1dzw
,
PDBe:1dzw
,
PDBj:1dzw
PDBsum
1dzw
PubMed
10821675
UniProt
P0AB87
|FUCA_ECOLI L-fuculose phosphate aldolase (Gene Name=fucA)
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