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3EPS

The crystal structure of isocitrate dehydrogenase kinase/phosphatase from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004674molecular_functionprotein serine/threonine kinase activity
A0004721molecular_functionphosphoprotein phosphatase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006006biological_processglucose metabolic process
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0008772molecular_function[isocitrate dehydrogenase (NADP+)] kinase activity
A0016208molecular_functionAMP binding
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016791molecular_functionphosphatase activity
B0000166molecular_functionnucleotide binding
B0004674molecular_functionprotein serine/threonine kinase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006006biological_processglucose metabolic process
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0008772molecular_function[isocitrate dehydrogenase (NADP+)] kinase activity
B0016208molecular_functionAMP binding
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0016791molecular_functionphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AMP A 1604
ChainResidue
AASN104
AASN377
ASER105
AHIS113
ALEU116
ALYS291
ALYS294
ATHR295
ATYR298
AGLU376

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 1605
ChainResidue
APRO316
AGLY317
AILE318
AVAL322
AMET323
AVAL325
ALYS336
AGLU416
AARG417
AARG418
AMET419
APRO421
AASN462
ATYR474
AASP475
AASP477
AGLU478
AMG1606

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1606
ChainResidue
AASN462
AASP475
AATP1605

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AMP B 1604
ChainResidue
BASN104
BSER105
BHIS113
BLEU116
BLYS291
BLYS294
BTHR295
BTYR298
BGLU376
BASN377
BHOH580

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP B 1605
ChainResidue
BPRO316
BGLY317
BILE318
BVAL322
BMET323
BVAL325
BVAL334
BLYS336
BGLU416
BARG417
BARG418
BMET419
BPRO421
BASN462
BTYR474
BASP475
BASP477
BGLU478
BHOH594
BMG1606

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 1606
ChainResidue
BASN462
BASP475
BATP1605

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747
ChainResidueDetails
AASP371
BASP371

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00747
ChainResidueDetails
AALA315
ALYS336
BALA315
BLYS336

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PDB entries from 2024-04-24

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