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2E0A

Crystal structure of human pyruvate dehydrogenase kinase 4 in complex with AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006885biological_processregulation of pH
A0008286biological_processinsulin receptor signaling pathway
A0009267biological_processcellular response to starvation
A0010510biological_processregulation of acetyl-CoA biosynthetic process from pyruvate
A0010565biological_processregulation of cellular ketone metabolic process
A0010906biological_processregulation of glucose metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0042304biological_processregulation of fatty acid biosynthetic process
A0042593biological_processglucose homeostasis
A0042594biological_processresponse to starvation
A0045124biological_processregulation of bone resorption
A0046320biological_processregulation of fatty acid oxidation
A0071398biological_processcellular response to fatty acid
A0072593biological_processreactive oxygen species metabolic process
A2000811biological_processnegative regulation of anoikis
B0004672molecular_functionprotein kinase activity
B0004740molecular_functionpyruvate dehydrogenase (acetyl-transferring) kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006885biological_processregulation of pH
B0008286biological_processinsulin receptor signaling pathway
B0009267biological_processcellular response to starvation
B0010510biological_processregulation of acetyl-CoA biosynthetic process from pyruvate
B0010565biological_processregulation of cellular ketone metabolic process
B0010906biological_processregulation of glucose metabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0042304biological_processregulation of fatty acid biosynthetic process
B0042593biological_processglucose homeostasis
B0042594biological_processresponse to starvation
B0045124biological_processregulation of bone resorption
B0046320biological_processregulation of fatty acid oxidation
B0071398biological_processcellular response to fatty acid
B0072593biological_processreactive oxygen species metabolic process
B2000811biological_processnegative regulation of anoikis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 500
ChainResidue
AGLU254
AASN258
AANP501
AHOH546
AHOH627

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 1500
ChainResidue
BASN258
BANP1501
BHOH1516
BHOH1624

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE ANP A 501
ChainResidue
AGLU254
AASN258
AARG261
AALA262
AASP293
AVAL298
ALEU306
ATYR311
ASER312
ATHR313
AALA328
AGLY329
APHE330
AGLY331
ATYR332
AGLY333
ALEU334
ATHR358
AMG500
AHOH504
AHOH505
AHOH512
AHOH527
AHOH546
AHOH574
AHOH580
AHOH594
AHOH620

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ANP B 1501
ChainResidue
BGLU254
BASN258
BARG261
BALA262
BASP293
BVAL298
BLEU306
BTYR311
BSER312
BTHR313
BALA328
BGLY329
BGLY331
BTYR332
BGLY333
BLEU334
BPRO335
BTHR358
BMG1500
BHOH1502
BHOH1507
BHOH1512
BHOH1520
BHOH1544
BHOH1599

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18658136
ChainResidueDetails
AGLU254
AASP293
ASER312
AGLY329
BGLU254
BASP293
BSER312
BGLY329

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Interaction with the other subunit in the homodimer
ChainResidueDetails
ATYR157
AARG161
ATRP395
BTYR157
BARG161
BTRP395

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1jm6
ChainResidueDetails
AGLU254
AHIS250

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1jm6
ChainResidueDetails
BGLU254
BHIS250

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PDB entries from 2024-08-28

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