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1ZJH

Structure of human muscle pyruvate kinase (PKM2)

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
A0016310biological_processphosphorylation
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
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE264-VAL276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AVAL70
APRO106
ALEU464

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
ALEU73
AILE270
AASP295
ALEU296
AGLN328

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
APHE75
AHIS77
ATHR113
ALYS114
ATHR120
AGLY207
AASN272

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
ChainResidueDetails
ALYS432
AALA482
AVAL489
APRO516

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
AILE270

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
ASER433

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
ALYS2

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
APRO3

site_idSWS_FT_FI9
Number of Residues1
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
APRO37

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AALA41

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AGLU62
AASN89

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ASER66
AALA498

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
APHE97
AASP100

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
AARG105

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLY127

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AMET148

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AVAL166
APRO322

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AVAL175

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AGLU195

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
AILE266

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AILE270

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
AVAL305

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
AILE403
ATHR408

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
ACYS423
ASER424

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ASER433

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AASP475

site_idSWS_FT_FI27
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
AGLY115

site_idSWS_FT_FI28
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
AILE266
AILE270

site_idSWS_FT_FI29
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
AVAL166

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ALYS269
ASER361
AARG119
AGLU363
AARG72
ATHR327

226707

PDB entries from 2024-10-30

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