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5WRP

T-state crystal structure of pyruvate kinase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PO4 A 501
ChainResidue
ATHR374
AGLN375
ASER376
ATHR379
AHOH620

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 B 501
ChainResidue
BTHR379
BHOH601
BTHR374
BGLN375
BSER376
BASP378

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 C 501
ChainResidue
CTHR374
CGLN375
CSER376
CASP378
CTHR379
CSER458

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 D 501
ChainResidue
DTHR374
DGLN375
DSER376
DASP378
DTHR379
DSER458
DHOH639

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. VpVIAKLEKpEAI
ChainResidueDetails
AVAL213-ILE225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG33
BASN35
BSER37
BASP67
BGLU220
BGLY243
BASP244
BTHR276
CARG33
CASN35
CSER37
AASN35
CASP67
CGLU220
CGLY243
CASP244
CTHR276
DARG33
DASN35
DSER37
DASP67
DGLU220
ASER37
DGLY243
DASP244
DTHR276
AASP67
AGLU220
AGLY243
AASP244
ATHR276
BARG33

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG74
ALYS155
BARG74
BLYS155
CARG74
CLYS155
DARG74
DLYS155

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
ALYS218
BLYS218
CLYS218
DLYS218

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PknJ; in vitro => ECO:0000269|PubMed:20520732
ChainResidueDetails
ASER37
BSER37
CSER37
DSER37

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PDB entries from 2024-07-10

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