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6NU5

Pyruvate Kinase M2 Mutant - S437Y in Complex with L-cysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005791cellular_componentrough endoplasmic reticulum
A0005829cellular_componentcytosol
A0005929cellular_componentcilium
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0012501biological_processprogrammed cell death
A0016301molecular_functionkinase activity
A0023026molecular_functionMHC class II protein complex binding
A0030955molecular_functionpotassium ion binding
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0034774cellular_componentsecretory granule lumen
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A1903561cellular_componentextracellular vesicle
A1903672biological_processpositive regulation of sprouting angiogenesis
A1904813cellular_componentficolin-1-rich granule lumen
A2000767biological_processpositive regulation of cytoplasmic translation
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0003824molecular_functioncatalytic activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005791cellular_componentrough endoplasmic reticulum
B0005829cellular_componentcytosol
B0005929cellular_componentcilium
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0012501biological_processprogrammed cell death
B0016301molecular_functionkinase activity
B0023026molecular_functionMHC class II protein complex binding
B0030955molecular_functionpotassium ion binding
B0031982cellular_componentvesicle
B0032869biological_processcellular response to insulin stimulus
B0034774cellular_componentsecretory granule lumen
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B1903561cellular_componentextracellular vesicle
B1903672biological_processpositive regulation of sprouting angiogenesis
B1904813cellular_componentficolin-1-rich granule lumen
B2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue CYS A 601
ChainResidue
AARG43
AHOH766
AHOH777
AASN44
AASN70
AARG106
AHIS464
AILE469
APHE470
APRO471
AHOH765

site_idAC2
Number of Residues12
Detailsbinding site for residue OXL A 602
ChainResidue
ALYS270
AGLU272
AALA293
AARG294
AGLY295
AASP296
ATHR328
AMG605
AHOH736
AHOH784
AHOH844
AHOH1055

site_idAC3
Number of Residues5
Detailsbinding site for residue SCN A 603
ChainResidue
ALYS266
AHIS439
ALEU465
ATYR466
AHOH905

site_idAC4
Number of Residues12
Detailsbinding site for residue B3P A 604
ChainResidue
AASP177
ALEU180
ALYS207
AGLN329
AGLU332
AGLY363
AHOH711
AHOH742
AHOH804
AHOH925
AHOH968
AHOH1025

site_idAC5
Number of Residues5
Detailsbinding site for residue MG A 605
ChainResidue
AGLU272
AASP296
AOXL602
AHOH784
AHOH844

site_idAC6
Number of Residues7
Detailsbinding site for residue K A 606
ChainResidue
AASN75
ASER77
AASP113
ATHR114
ASER243
AHOH904
AHOH1055

site_idAC7
Number of Residues12
Detailsbinding site for residue CYS B 601
ChainResidue
BARG43
BASN44
BASN70
BARG106
BHIS464
BILE469
BPHE470
BPRO471
BHOH747
BHOH784
BHOH792
BHOH822

site_idAC8
Number of Residues11
Detailsbinding site for residue OXL B 602
ChainResidue
BLYS270
BGLU272
BALA293
BARG294
BGLY295
BASP296
BTHR328
BMG607
BHOH720
BHOH827
BHOH884

site_idAC9
Number of Residues6
Detailsbinding site for residue SCN B 603
ChainResidue
BLYS266
BPRO323
BHIS439
BLEU465
BTYR466
BHOH851

site_idAD1
Number of Residues13
Detailsbinding site for residue B3P B 604
ChainResidue
ALYS337
BASP177
BASP178
BLEU180
BLYS207
BGLN329
BGLU332
BGLY363
BHOH736
BHOH798
BHOH803
BHOH916
BHOH978

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO B 605
ChainResidue
BARG255
BALA286
AHIS81
AGLU82
APHE231
BVAL251
BHIS252

site_idAD3
Number of Residues7
Detailsbinding site for residue EDO B 606
ChainResidue
AHOH998
BPHE26
BHIS29
BLEU33
BLEU353
BALA388
BHOH704

site_idAD4
Number of Residues5
Detailsbinding site for residue MG B 607
ChainResidue
BGLU272
BASP296
BOXL602
BHOH827
BHOH884

site_idAD5
Number of Residues6
Detailsbinding site for residue K B 608
ChainResidue
BASN75
BSER77
BASP113
BTHR114
BHOH778
BHOH1078

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE265-VAL277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AASN70
AARG106
AHIS464
BASN70
BARG106
BHIS464

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
BLYS270
BGLY295
BASP296
BTHR328
AARG73
ALYS270
AGLY295
AASP296
ATHR328
BARG73

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
AASP113
ATHR114
AARG120
ALYS207
AGLU272
BASN75
BSER77
BASP113
BTHR114
BARG120
BLYS207
BGLU272
AASN75
ASER77

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
ChainResidueDetails
BTHR432
BTRP482
BARG489
BARG516
ATHR432
ATRP482
AARG489
AARG516

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS270
BLYS270

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
ALYS433
BLYS433

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS3
BLYS3

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER37
BSER37

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR41
BTHR41

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS62
BLYS89
ALYS62
ALYS89

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
BLYS66
BLYS498
ALYS66
ALYS498

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
BSER97
BSER100
ASER97
ASER100

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTYR105
ATYR105

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER127
ASER127

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ATYR148
BTYR148

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
BLYS322
ALYS166
ALYS322
BLYS166

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR175
ATYR175

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BTHR195
ATHR195

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS266
ALYS266

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
BLYS270
ALYS270

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
BLYS305
ALYS305

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
BPRO403
BPRO408
APRO403
APRO408

site_idSWS_FT_FI24
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
ACYS423
BCYS423
BCYS424
ACYS424

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS433
BLYS433

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS475
BLYS475

site_idSWS_FT_FI27
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS115
ALYS115

site_idSWS_FT_FI28
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS270
BLYS266
BLYS270
ALYS266

site_idSWS_FT_FI29
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS166
BLYS166

221051

PDB entries from 2024-06-12

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