Structure of PDB 5ucz Chain B Binding Site BS01

Receptor Information
>5ucz Chain B (length=291) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLVKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASE
GAIKYMGIDMAVGMVKIMCERYPHIPVALHLDHGTTFESCEKAVKAGFTS
VMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGVLVNPKEAEQFVKE
SQVDYLAPAIGTSHGAFKFKGEPKLDFERLQEVKRLTNIPLVLHGASAIP
DNVRKSYLDAGGDLKGSKGVPFEFLQESVKGGINKVNTDTDLRIAFIAEV
RKVANEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANKI
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5ucz Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ucz Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
Resolution1.78 Å
Binding residue
(original residue number in PDB)		H83 H180 H210
Binding residue
(residue number reindexed from 1)		H83 H164 H194
Annotation score1
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:5ucz, PDBe:5ucz, PDBj:5ucz
PDBsum5ucz
PubMed29593097
UniProtP56109|ALF_HELPY Fructose-bisphosphate aldolase (Gene Name=fba)

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