Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5WS8

Pyruvate kinase (PYK) from Mycobacterium tuberculosis in complex with Oxalate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide 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
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide 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
C0016740molecular_functiontransferase activity
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide 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
D0016740molecular_functiontransferase activity
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 501
ChainResidue
ALYS218
AGLU220
AASP244
AOXL502
AHOH612
AHOH637

site_idAC2
Number of Residues12
Detailsbinding site for residue OXL A 502
ChainResidue
AARG242
AGLY243
AASP244
ATHR276
AMG501
AHOH612
AHOH615
AHOH637
AHOH678
ALYS218
AGLU220
AALA241

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 501
ChainResidue
BLYS218
BGLU220
BASP244
BOXL502
BHOH610
BHOH639

site_idAC4
Number of Residues9
Detailsbinding site for residue OXL B 502
ChainResidue
BLYS218
BGLU220
BALA241
BARG242
BGLY243
BASP244
BTHR276
BMG501
BHOH639

site_idAC5
Number of Residues6
Detailsbinding site for residue MG C 501
ChainResidue
CLYS218
CGLU220
CASP244
COXL502
CHOH603
CHOH674

site_idAC6
Number of Residues11
Detailsbinding site for residue OXL C 502
ChainResidue
CLYS218
CGLU220
CALA241
CARG242
CGLY243
CASP244
CTHR276
CMG501
CHOH603
CHOH645
CHOH674

site_idAC7
Number of Residues6
Detailsbinding site for residue MG D 501
ChainResidue
DLYS218
DGLU220
DASP244
DOXL502
DHOH607
DHOH647

site_idAC8
Number of Residues9
Detailsbinding site for residue OXL D 502
ChainResidue
DLYS218
DGLU220
DALA241
DARG242
DGLY243
DASP244
DTHR276
DMG501
DHOH647

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 site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PknJ; in vitro","evidences":[{"source":"PubMed","id":"20520732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon