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3EOL

2.0A crystal structure of isocitrate lyase from Brucella melitensis (P43212)

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 430
ChainResidue
AILE200
AARG238
ATYR274
AHOH454
AHOH529

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 430
ChainResidue
BTYR245
BARG330

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG B 431
ChainResidue
BARG238
BALA270
BTYR274
BHOH444
BHOH477
BALA197
BILE200

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL
ChainResidueDetails
ALYS183-LEU188

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PDB entries from 2024-06-12

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