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6KSH

Crystal structure of pyruvate kinase (PYK) from Plasmodium falciparum in complex with oxalate and ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 601
ChainResidue
AGLU257
AASP281
AATP603
AOXL605
AHOH773

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 602
ChainResidue
AATP603
AHOH714
AHOH745
AHOH794

site_idAC3
Number of Residues29
Detailsbinding site for residue ATP A 603
ChainResidue
ATHR44
ALEU45
APRO47
AARG67
AASN69
AHIS72
AHIS78
AARG109
ALYS191
AASN192
ALYS255
AASP281
ASER347
AGLY348
AALA351
AMG601
AMG602
AK604
AOXL605
AHOH708
AHOH710
AHOH714
AHOH721
AHOH745
AHOH763
AHOH794
AHOH832
AHOH839
AHOH852

site_idAC4
Number of Residues7
Detailsbinding site for residue K A 604
ChainResidue
AASN69
ASER71
AASP102
ATHR103
ASER228
AATP603
AHOH704

site_idAC5
Number of Residues11
Detailsbinding site for residue OXL A 605
ChainResidue
ALYS255
AGLU257
AALA278
AARG279
AGLY280
AASP281
ATHR313
AMG601
AATP603
AHOH714
AHOH794

site_idAC6
Number of Residues5
Detailsbinding site for residue MG B 601
ChainResidue
BGLU257
BASP281
BATP603
BOXL605
BHOH754

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 602
ChainResidue
BSER347
BATP603
BHOH705
BHOH708
BHOH743

site_idAC8
Number of Residues24
Detailsbinding site for residue ATP B 603
ChainResidue
BTHR44
BLEU45
BPRO47
BARG67
BASN69
BHIS72
BHIS78
BARG109
BLYS191
BASN192
BLYS255
BASP281
BSER347
BALA351
BMG601
BMG602
BK604
BOXL605
BHOH705
BHOH715
BHOH730
BHOH735
BHOH743
BHOH806

site_idAC9
Number of Residues6
Detailsbinding site for residue K B 604
ChainResidue
BASN69
BSER71
BASP102
BTHR103
BSER228
BATP603

site_idAD1
Number of Residues12
Detailsbinding site for residue OXL B 605
ChainResidue
BARG279
BGLY280
BASP281
BTHR313
BMG601
BATP603
BHOH705
BHOH708
BHOH754
BLYS255
BGLU257
BALA278

site_idAD2
Number of Residues5
Detailsbinding site for residue MG C 601
ChainResidue
CGLU257
CASP281
CATP603
COXL605
CHOH715

site_idAD3
Number of Residues4
Detailsbinding site for residue MG C 602
ChainResidue
CATP603
CHOH729
CHOH731
CHOH732

site_idAD4
Number of Residues23
Detailsbinding site for residue ATP C 603
ChainResidue
CTHR44
CLEU45
CPRO47
CARG67
CASN69
CHIS72
CARG109
CLYS191
CASN192
CLYS255
CASP281
CSER347
CALA351
CMG601
CMG602
CK604
COXL605
CHOH702
CHOH722
CHOH731
CHOH732
CHOH769
CHOH812

site_idAD5
Number of Residues7
Detailsbinding site for residue K C 604
ChainResidue
CASN69
CSER71
CASP102
CTHR103
CSER228
CATP603
CHOH707

site_idAD6
Number of Residues11
Detailsbinding site for residue OXL C 605
ChainResidue
CLYS255
CGLU257
CALA278
CARG279
CGLY280
CASP281
CTHR313
CMG601
CATP603
CHOH715
CHOH732

site_idAD7
Number of Residues5
Detailsbinding site for residue MG D 601
ChainResidue
DGLU257
DASP281
DATP603
DOXL605
DHOH712

site_idAD8
Number of Residues4
Detailsbinding site for residue MG D 602
ChainResidue
DATP603
DHOH706
DHOH742
DHOH809

site_idAD9
Number of Residues28
Detailsbinding site for residue ATP D 603
ChainResidue
DTHR44
DLEU45
DPRO47
DARG67
DASN69
DHIS72
DHIS78
DASP102
DARG109
DLYS191
DASN192
DLYS255
DASP281
DSER347
DGLY348
DALA351
DMG601
DMG602
DK604
DOXL605
DHOH706
DHOH707
DHOH709
DHOH742
DHOH752
DHOH756
DHOH809
DHOH818

site_idAE1
Number of Residues7
Detailsbinding site for residue K D 604
ChainResidue
DASN69
DSER71
DASP102
DTHR103
DSER228
DATP603
DHOH738

site_idAE2
Number of Residues12
Detailsbinding site for residue OXL D 605
ChainResidue
DLYS255
DGLU257
DALA278
DARG279
DGLY280
DASP281
DTHR313
DMG601
DATP603
DHOH712
DHOH742
DHOH809

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIIPKIENiEGI
ChainResidueDetails
AILE250-ILE262

226707

PDB entries from 2024-10-30

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