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4IQE

Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor

Replaces:  3KZ2
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
A0046421molecular_functionmethylisocitrate lyase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0016829molecular_functionlyase activity
B0016833molecular_functionoxo-acid-lyase activity
B0019629biological_processpropionate catabolic process, 2-methylcitrate cycle
B0046421molecular_functionmethylisocitrate lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL
ChainResidueDetails
ALYS127-LEU132

219140

PDB entries from 2024-05-01

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