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6ITO

Crystal structure of pyruvate kinase (PYK) from Mycobacterium tuberculosis in complex with Oxalate, AMP and inhibitor Ribose 5-Phosphate

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 MG A 501
ChainResidue
AGLU220
AASP244
AOXL502
AHOH602
AHOH607

site_idAC2
Number of Residues11
Detailsbinding site for residue OXL A 502
ChainResidue
AGLY243
AASP244
ATHR276
AMG501
AHOH602
AHOH604
AHOH607
ALYS218
AGLU220
AALA241
AARG242

site_idAC3
Number of Residues9
Detailsbinding site for residue R5P A 503
ChainResidue
AGLU267
AASN268
AHIS345
APRO347
AARG348
ATHR349
AGLY352
AARG382
AARG385

site_idAC4
Number of Residues20
Detailsbinding site for residue AMP A 504
ChainResidue
AARG351
APHE373
ATHR374
AGLN375
ASER376
ATHR379
AALA397
AVAL416
APRO417
ALYS418
AMET419
AMET425
AGLY450
APRO453
AGLY454
ATHR455
AVAL456
AGLY457
ASER458
ATHR459

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 501
ChainResidue
BLYS218
BGLU220
BASP244
BOXL502
BHOH603
BHOH633

site_idAC6
Number of Residues9
Detailsbinding site for residue OXL B 502
ChainResidue
BLYS218
BGLU220
BALA241
BARG242
BGLY243
BASP244
BTHR276
BMG501
BHOH633

site_idAC7
Number of Residues9
Detailsbinding site for residue R5P B 503
ChainResidue
BGLU267
BASN268
BHIS345
BPRO347
BARG348
BTHR349
BGLY352
BARG382
BARG385

site_idAC8
Number of Residues19
Detailsbinding site for residue AMP B 504
ChainResidue
BARG351
BPHE373
BTHR374
BGLN375
BSER376
BTHR379
BALA397
BVAL416
BPRO417
BLYS418
BMET419
BMET425
BGLY450
BPRO453
BGLY454
BTHR455
BGLY457
BSER458
BTHR459

site_idAC9
Number of Residues5
Detailsbinding site for residue MG C 501
ChainResidue
CGLU220
CASP244
COXL502
CHOH607
CHOH612

site_idAD1
Number of Residues8
Detailsbinding site for residue OXL C 502
ChainResidue
CTHR276
CMG501
CLYS218
CGLU220
CALA241
CARG242
CGLY243
CASP244

site_idAD2
Number of Residues9
Detailsbinding site for residue R5P C 503
ChainResidue
CGLU267
CASN268
CHIS345
CPRO347
CARG348
CTHR349
CGLY352
CARG382
CARG385

site_idAD3
Number of Residues20
Detailsbinding site for residue AMP C 504
ChainResidue
CARG351
CPHE373
CTHR374
CGLN375
CSER376
CTHR379
CALA397
CVAL416
CPRO417
CLYS418
CMET419
CMET425
CGLY450
CPRO453
CGLY454
CTHR455
CVAL456
CGLY457
CSER458
CTHR459

site_idAD4
Number of Residues6
Detailsbinding site for residue MG D 501
ChainResidue
DLYS218
DGLU220
DASP244
DOXL502
DHOH602
DHOH607

site_idAD5
Number of Residues9
Detailsbinding site for residue OXL D 502
ChainResidue
DLYS218
DGLU220
DALA241
DARG242
DGLY243
DASP244
DTHR276
DMG501
DHOH602

site_idAD6
Number of Residues10
Detailsbinding site for residue R5P D 503
ChainResidue
DGLU267
DASN268
DHIS345
DPRO347
DARG348
DTHR349
DGLY352
DARG382
DARG385
DHOH615

site_idAD7
Number of Residues20
Detailsbinding site for residue AMP D 504
ChainResidue
DARG351
DPHE373
DTHR374
DGLN375
DSER376
DTHR379
DPHE395
DALA397
DVAL416
DPRO417
DLYS418
DMET419
DMET425
DGLY450
DGLY454
DTHR455
DVAL456
DGLY457
DSER458
DTHR459

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 2024-07-17

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