Structure of PDB 3c56 Chain A

Receptor sequence
>3c56A (length=297) Species: 210 (Helicobacter pylori) [Search protein sequence]
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASE
GAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTS
VMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIAVLVNPKEA
EQFVKESQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLH
GASAIPDNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRI
AFIAEVRKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
3D structure
PDB3c56 Synthesis and Biochemical Evaluation of Selective Inhibitors of Class II Fructose Bisphosphate Aldolases: Towards New Synthetic Antibiotics.
ChainA
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 H170 A216 N243
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 H180 H210 H83 H170 H200
BS02 PH4 A N23 S49 D82 H180 K184 G211 S213 N253 D255 T256 R259 N23 S49 D82 H170 K174 G201 S203 N243 D245 T246 R249 MOAD: Ki=0.013uM
PDBbind-CN: -logKd/Ki=7.89,Ki=0.013uM
BindingDB: Ki=13nM
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:3c56, PDBe:3c56, PDBj:3c56
PDBsum3c56
PubMed18688832
UniProtP56109|ALF_HELPY Fructose-bisphosphate aldolase (Gene Name=fba)

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