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8G2E

PKM2 bound to compound 2

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
AILE265-VAL277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AASN70
AARG106
AHIS464

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AARG73
ALYS270
AGLY295
AASP296
ATHR328

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
AASN75
ASER77
AASP113
ATHR114
AARG120
ALYS207
AGLU272

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
ATHR432
ATRP482
AARG489
AARG516

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS270

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
ALYS433

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
ASER2

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS3

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
ASER37

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR41

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS62
ALYS89

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS66
ALYS498

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
ASER97
ASER100

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR105

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER127

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ATYR148

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS166
ALYS322

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR175

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR195

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS266

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS270

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
ALYS305

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
APRO403
APRO408

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
ACYS423
ACYS424

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS433

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS475

site_idSWS_FT_FI27
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS115

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
ALYS266
ALYS270

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
ALYS166

226707

PDB entries from 2024-10-30

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