Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T65889 | Target Info | |||
| Target Name | Pyruvate kinase M2 (PKM) | ||||
| Synonyms | p58; Tumor M2-PK; Thyroid hormone-binding protein 1; THBP1; Pyruvate kinase muscle isozyme; Pyruvate kinase isozymes M1/M2; Pyruvate kinase PKM; Pyruvate kinase 2/3; PKM2; PK3; PK2; Opa-interacting protein 3; OIP3; OIP-3; Cytosolic thyroid hormone-binding protein; CTHBP | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | PKM | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Pyruvic acid | Ligand Info | |||
| Canonical SMILES | CC(=O)C(=O)O | ||||
| InChI | 1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6) | ||||
| InChIKey | LCTONWCANYUPML-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 1060 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4YJ5 Crystal structure of PKM2 mutant | ||||||
| Method | X-ray diffraction | Resolution | 2.41 Å | Mutation | Yes | [1] |
| PDB Sequence |
QTQQLHAAMA
23 DTFLEHMCRL33 DIDSPPITAR43 NTGIICTIGP53 ASRSVETLKE63 MIKSGMNVAR 73 LNFSHGTHEY83 HAETIKNVRT93 ATESFASDPI103 LYRPVAVALD113 TKGPEIRTGL 123 IKGSGTAEVE133 LKKGATLKIT143 LDNAYMEKCD153 ENILWLDYKN163 ICKVVEVGSK 173 IYVDDGLISL183 QVKQKGADFL193 VTEVENGGSL203 GSKKGVNLPG213 AAVDLPAVSE 223 KDIQDLKFGV233 EQDVDMVFAS243 FIRKASDVHE253 VRKVLGEKGK263 NIKIISKIEN 273 HEGVRRFDEI283 LEASDGIMVA293 RGDLGIEIPA303 EKVFLAQKMM313 IGRCNRAGKP 323 VICATQMLES333 MIKKPRPTRA343 EGSDVANAVL353 DGADCIMLSG363 ETAKGDYPLE 373 AVRMQHLIAR383 EAEAAIYYLQ393 LFEELRRLAP403 ITSDPTEATA413 VGAVEASFKC 423 CSGAIIVLTK433 SGRSAHQVAR443 YRPRAPIIAV453 TRNPQTARQA463 HLYRGIFPVL 473 CKDPVQEAWA483 EDVDLRVNFA493 MNVGKARGFF503 KKGDVVIVLT513 GWRPGSGFTN 523 TMRVVPVP
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| PDB ID: 5X0I Crystal structure of PKM2 R399E mutant complexed with FBP and serine | ||||||
| Method | X-ray diffraction | Resolution | 2.64 Å | Mutation | Yes | [2] |
| PDB Sequence |
QTQQLHAAMA
23 DTFLEHMCRL33 DIDSPPITAR43 NTGIICTIGP53 ASRSVETLKE63 MIKSGMNVAR 73 LNFSHGTHEY83 HAETIKNVRT93 ATESFASDPI103 LYRPVAVALD113 TKGPEIRTGL 123 IKGSGTAEVE133 LKKGATLKIT143 LDNAYMEKCD153 ENILWLDYKN163 ICKVVEVGSK 173 IYVDDGLISL183 QVKQKGADFL193 VTEVENGGSL203 GSKKGVNLPG213 AAVDLPAVSE 223 KDIQDLKFGV233 EQDVDMVFAS243 FIRKASDVHE253 VRKVLGEKGK263 NIKIISKIEN 273 HEGVRRFDEI283 LEASDGIMVA293 RGDLGIEIPA303 EKVFLAQKMM313 IGRCNRAGKP 323 VICATQMLES333 MIKKPRPTRA343 EGSDVANAVL353 DGADCIMLSG363 ETAKGDYPLE 373 AVRMQHLIAR383 EAEAAIYHLQ393 LFEELERLAP403 ITSDPTEATA413 VGAVEASFKC 423 CSGAIIVLTK433 SGRSAHQVAR443 YRPRAPIIAV453 TRNPQTARQA463 HLYRGIFPVL 473 CKDPVQEAWA483 EDVDLRVNFA493 MNVGKARGFF503 KKGDVVIVLT513 GWRPGSGFTN 523 TMRVVPVP
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| PDB ID: 3SRF Human M1 pyruvate kinase | ||||||
| Method | X-ray diffraction | Resolution | 2.85 Å | Mutation | No | [3] |
| PDB Sequence |
IQTQQLHAAM
21 ADTFLEHMCR31 LDIDSPPITA41 RNTGIICTIG51 PASRSVETLK61 EMIKSGMNVA 71 RLNFSHGTHE81 YHAETIKNVR91 TATESFASDP101 ILYRPVAVAL111 DTKGPEIRTG 121 LIKGTAEVEL133 KKGATLKITL143 DNAYMEKCDE153 NILWLDYKNI163 CKVVEVGSKI 173 YVDDGLISLQ183 VKQKGADFLV193 TEVENGGSLG203 SKKGVNLPGA213 AVDLPAVSEK 223 DIQDLKFGVE233 QDVDMVFASF243 IRKASDVHEV253 RKVLGEKGKN263 IKIISKIENH 273 EGVRRFDEIL283 EASDGIMVAR293 GDLGIEIPAE303 KVFLAQKMMI313 GRCNRAGKPV 323 ICATQMLESM333 IKKPRPTRAE343 GSDVANAVLD353 GADCIMLSGE363 TAKGDYPLEA 373 VRMQHLIARE383 AEAAMFHRKL393 FEELVRASSH403 STDLMEAMAM413 GSVEASYKCL 423 AAALIVLTES433 GRSAHQVARY443 RPRAPIIAVT453 RNPQTARQAH463 LYRGIFPVLC 473 KDPVQEAWAE483 DVDLRVNFAM493 NVGKARGFFK503 KGDVVIVLTG513 WRPGSGFTNT 523 MRVVPVP
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Mutations in the PKM2 exon-10 region are associated with reduced allostery and increased nuclear translocation. doi:10.1038/s42003-019-0343-4. | ||||
| REF 2 | Mutations in the PKM2 exon-10 region are associated with reduced allostery and increased nuclear translocation. Commun Biol. 2019 Mar 15;2:105. | ||||
| REF 3 | Allosetric regulation of M2 pyruvate kinase. | ||||
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