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3T0T

Crystal structure of S. aureus Pyruvate Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE I30 A 586
ChainResidue
ATHR353
BTHR366
BASN369
AALA358
AILE361
ASER362
AHIS365
AASN369
BILE361
BSER362
BHIS365

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE I30 D 586
ChainResidue
CALA358
CILE361
CSER362
CHIS365
CASN369
DILE361
DSER362
DHIS365
DTHR366
DASN369

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 587
ChainResidue
AALA378
ATHR379
AGLU380
ASER381
AGLY382
ASER383
ATHR384
ATHR461
AGLY462

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 586
ChainResidue
BTHR379
BGLU380
BSER381
BGLY382
BSER383
BTHR384
BTHR461

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 C 586
ChainResidue
CALA378
CTHR379
CSER381
CGLY382
CSER383
CTHR384
CTHR461
CGLY462

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D 587
ChainResidue
DTHR379
DGLU380
DSER381
DGLY382
DSER383
DTHR384
DTHR461
DGLY462

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG32
BARG32
BASN34
BSER36
BASP66
BTHR67
BGLU221
BGLY244
BASP245
BTHR277
CARG32
AASN34
CASN34
CSER36
CASP66
CTHR67
CGLU221
CGLY244
CASP245
CTHR277
DARG32
DASN34
ASER36
DSER36
DASP66
DTHR67
DGLU221
DGLY244
DASP245
DTHR277
AASP66
ATHR67
AGLU221
AGLY244
AASP245
ATHR277

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG73
ALYS156
BARG73
BLYS156
CARG73
CLYS156
DARG73
DLYS156

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
ALYS219
BLYS219
CLYS219
DLYS219

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PDB entries from 2024-11-06

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