Structure of PDB 3c52 Chain B

Receptor sequence
>3c52B (length=295) Species: 210 (Helicobacter pylori) [Search protein sequence]
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASE
GAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTS
VMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGILVNPKEAEQ
FVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGA
SAIPDNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAF
IAEVRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
3D structure
PDB3c52 Synthesis and Biochemical Evaluation of Selective Inhibitors of Class II Fructose Bisphosphate Aldolases: Towards New Synthetic Antibiotics.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C69 E70 G136 H180 A226 N253
Catalytic site (residue number reindexed from 1) C69 E70 G136 H168 A214 N241
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 B H83 H180 H210 H83 H168 H198
BS02 CA B D104 S106 E134 D104 S106 E134
BS03 PGH B D82 H83 H180 K184 H210 G211 S213 N253 D255 T256 D82 H83 H168 K172 H198 G199 S201 N241 D243 T244 PDBbind-CN: -logKd/Ki=7.30,Ki=0.05uM
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:3c52, PDBe:3c52, PDBj:3c52
PDBsum3c52
PubMed18688832
UniProtP56109|ALF_HELPY Fructose-bisphosphate aldolase (Gene Name=fba)

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