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3I4E

Crystal structure of Isocitrate Lyase from Burkholderia pseudomallei

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004451molecular_functionisocitrate lyase activity
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004451molecular_functionisocitrate lyase activity
C0016829molecular_functionlyase activity
C0019752biological_processcarboxylic acid metabolic process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0016829molecular_functionlyase activity
D0019752biological_processcarboxylic acid metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM
ChainResidueDetails
ALYS190-MET195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
AHIS181
ACYS192
AARG229

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
BHIS181
BCYS192
BARG229

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
CHIS181
CCYS192
CARG229

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
DHIS181
DCYS192
DARG229

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PDB entries from 2024-07-24

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