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3E5B

2.4 A crystal structure of isocitrate lyase from brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0009514cellular_componentglyoxysome
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004451molecular_functionisocitrate lyase activity
B0009514cellular_componentglyoxysome
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004451molecular_functionisocitrate lyase activity
C0009514cellular_componentglyoxysome
C0016829molecular_functionlyase activity
C0019752biological_processcarboxylic acid metabolic process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0009514cellular_componentglyoxysome
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. KKCGHL
ChainResidueDetails
ALYS183-LEU188

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
AHIS174
AARG222

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
BHIS174
BARG222

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
CHIS174
CARG222

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8m
ChainResidueDetails
DHIS174
DARG222

222036

PDB entries from 2024-07-03

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