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7EBF

Cryo-EM structure of Isocitrate lyase-1 from Candida albicans

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0005737cellular_componentcytoplasm
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0009514cellular_componentglyoxysome
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046421molecular_functionmethylisocitrate lyase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004451molecular_functionisocitrate lyase activity
B0005737cellular_componentcytoplasm
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0009514cellular_componentglyoxysome
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046421molecular_functionmethylisocitrate lyase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004451molecular_functionisocitrate lyase activity
C0005737cellular_componentcytoplasm
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0009514cellular_componentglyoxysome
C0016829molecular_functionlyase activity
C0019752biological_processcarboxylic acid metabolic process
C0046421molecular_functionmethylisocitrate lyase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0005737cellular_componentcytoplasm
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0009514cellular_componentglyoxysome
D0016829molecular_functionlyase activity
D0019752biological_processcarboxylic acid metabolic process
D0046421molecular_functionmethylisocitrate lyase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM
ChainResidueDetails
ALYS208-MET213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKK7
ChainResidueDetails
ACYS210
BCYS210
CCYS210
DCYS210

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WKK7
ChainResidueDetails
ASER101
BARG247
BASN430
BTHR464
CSER101
CASP172
CGLY211
CARG247
CASN430
CTHR464
DSER101
AASP172
DASP172
DGLY211
DARG247
DASN430
DTHR464
AGLY211
AARG247
AASN430
ATHR464
BSER101
BASP172
BGLY211

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PDB entries from 2024-07-17

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