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9HHS

Crystal Structure of the Coxiella burnetii R152Q Mutant 2-methylisocitrate lyase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
A0046421molecular_functionmethylisocitrate lyase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
B0046421molecular_functionmethylisocitrate lyase activity
Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR
ChainResidueDetails
ALYS116-ARG121

251174

PDB entries from 2026-03-25

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