Structure of PDB 7x78 Chain A Binding Site BS03

Receptor Information
>7x78 Chain A (length=203) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MERNRLARQIIDTCLEMTRLGLNAGNVSVRYQGGMLITPTGIPYEKLTED
KIVFIDADGQHEQGKLPSSEWRFHQAAYQTRPDAQAVVHNHAVHCTAVSI
LNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVAVALKHRKATLLQ
HHGLIACEASLEKALWLAHEVEVLAQLYLSTLAITDPVPVLDDEAIAIVL
EKF
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain7x78 Chain A Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7x78 Structural characterization of an L-fuculose-1-phosphate aldolase from Klebsiella pneumoniae.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		H64 Q66
Binding residue
(residue number reindexed from 1)		H61 Q63
Annotation score1
Enzymatic activity
Enzyme Commision number 4.1.2.17: L-fuculose-phosphate aldolase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008738 L-fuculose-phosphate aldolase activity
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005996 monosaccharide metabolic process
GO:0006004 fucose metabolic process
GO:0019317 fucose catabolic process
GO:0019323 pentose catabolic process
GO:0019568 arabinose catabolic process
GO:0042355 L-fucose catabolic process
Cellular Component
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:7x78, PDBe:7x78, PDBj:7x78
PDBsum7x78
PubMed35366538
UniProtA6TD81

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