Structure of PDB 5ucp Chain A Binding Site BS03
Receptor Information
>5ucp Chain A (length=292) Species:
85962
(Helicobacter pylori 26695) [
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MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASE
GAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTS
VMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRVLVNPKEAEQFVK
ESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAI
PDNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAE
VRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
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
5ucp Chain A Residue 404 [
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Receptor-Ligand Complex Structure
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PDB
5ucp
Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
Resolution
1.444 Å
Binding residue
(original residue number in PDB)
H83 H180
Binding residue
(residue number reindexed from 1)
H83 H165
Annotation score
1
Enzymatic activity
Enzyme Commision number
4.1.2.13
: fructose-bisphosphate aldolase.
Gene Ontology
Molecular Function
GO:0004332
fructose-bisphosphate aldolase activity
GO:0008270
zinc ion binding
GO:0016829
lyase activity
GO:0016832
aldehyde-lyase activity
GO:0046872
metal ion binding
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0006096
glycolytic process
GO:0030388
fructose 1,6-bisphosphate metabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:5ucp
,
PDBe:5ucp
,
PDBj:5ucp
PDBsum
5ucp
PubMed
29593097
UniProt
P56109
|ALF_HELPY Fructose-bisphosphate aldolase (Gene Name=fba)
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