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2ZKJ

Crystal structure of human PDK4-ADP complex

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
AASN258
AADP501
APO4502
AHOH521
AHOH597

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AGLY329
APHE330
AGLY331
ATYR332
AGLY333
AMG500
AADP501
AHOH597
AGLU254
ALYS257
ALEU327
AALA328

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 500
ChainResidue
BASN258
BADP501
BPO4502
BHOH506
BHOH517

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BGLU254
BLYS257
BLEU327
BALA328
BGLY331
BTYR332
BGLY333
BMG500
BADP501
BHOH517

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP A 501
ChainResidue
AASN258
AARG261
AALA262
AASP293
AVAL298
ALEU306
ATYR311
ASER312
ATHR313
AALA328
AGLY329
APHE330
AGLY331
AGLY333
ALEU334
ATHR358
AMG500
APO4502
AHOH503
AHOH509
AHOH513
AHOH521
AHOH524
AHOH559

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP B 501
ChainResidue
BASN258
BARG261
BALA262
BASP293
BVAL298
BLEU306
BTYR311
BSER312
BTHR313
BALA328
BGLY329
BPHE330
BGLY331
BGLY333
BLEU334
BTHR358
BMG500
BPO4502
BHOH503
BHOH506
BHOH512
BHOH516
BHOH524
BHOH552

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 2024-10-30

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