Structure of PDB 5uck Chain A

Receptor sequence
>5uckA (length=291) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASE
GAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTS
VMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLVNPKEAEQFVKE
SQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAIP
DNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAEV
RKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
3D structure
PDB5uck Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
ChainA
Resolution1.782 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 ZN A H83 E134 H210 H83 E134 H194
BS02 ZN A H83 H180 H210 H83 H164 H194
BS03 G3H A S49 D82 H83 H180 D255 R259 S49 D82 H83 H164 D239 R243
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:5uck, PDBe:5uck, PDBj:5uck
PDBsum5uck
PubMed29593097
UniProtP56109|ALF_HELPY Fructose-bisphosphate aldolase (Gene Name=fba)

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