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 | L-phenylalanine | Ligand Info | |||
| Canonical SMILES | C1=CC=C(C=C1)CC(C(=O)O)N | ||||
| InChI | 1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1 | ||||
| InChIKey | COLNVLDHVKWLRT-QMMMGPOBSA-N | ||||
| PubChem Compound ID | 6140 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6GG4 Crystal structure of M2 PYK in complex with Phenyalanine. | ||||||
| Method | X-ray diffraction | Resolution | 2.46 Å | Mutation | No | [1] |
| PDB Sequence |
ADTFLEHMCR
32 LDIDSPPITA42 RNTGIICTIG52 PASRSVETLK62 EMIKSGMNVA72 RLNFSHGTHE 82 YHAETIKNVR92 TATESFASDP102 ILYRPVAVAL112 DTKGPEIRTG122 LIKGSGTAEV 132 ELKKGATLKI142 TLDNAYMEKC152 DENILWLDYK162 NICKVVEVGS172 KIYVDDGLIS 182 LQVKQKGADF192 LVTEVENGGS202 LGSKKGVNLP212 GAAVDLPAVS222 EKDIQDLKFG 232 VEQDVDMVFA242 SFIRKASDVH252 EVRKVLGEKG262 KNIKIISKIE272 NHEGVRRFDE 282 ILEASDGIMV292 ARGDLGIEIP302 AEKVFLAQKM312 MIGRCNRAGK322 PVICATQMLE 332 SMIKKPRPTR342 AEGSDVANAV352 LDGADCIMLS362 GETAKGDYPL372 EAVRMQHLIA 382 REAEAAIYHL392 QLFEELRRLA402 PITSDPTEAT412 AVGAVEASFK422 CCSGAIIVLT 432 KSGRSAHQVA442 RYRPRAPIIA452 VTRNPQTARQ462 AHLYRGIFPV472 LKDPVQEAWA 483 EDVDLRVNFA493 MNVGKARGFF503 KKGDVVIVLT513 GWRPGSGFTN523 TMRVVPVP |
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| PDB ID: 4FXJ Structure of M2 pyruvate kinase in complex with phenylalanine | ||||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [2] |
| PDB Sequence |
EHMCRLDIDS
37 PPITARNTGI47 ICTIGPASRS57 VETLKEMIKS67 GMNVARLNFS77 HGTHEYHAET 87 IKNVRTATES97 FASDPILYRP107 VAVALDTKGP117 EIRTGLIKGA130 EVELKKGATL 140 KITLDNAYME150 KCDENILWLD160 YKNICKVVEV170 GSKIYVDDGL180 ISLQVKQKGA 190 DFLVTEVENG200 GSLGSKKGVN210 LPGAAVDLPA220 VSEKDIQDLK230 FGVEQDVDMV 240 FASFIRKASD250 VHEVRKVLGE260 KGKNIKIISK270 IENHEGVRRF280 DEILEASDGI 290 MVARGDLGIE300 IPAEKVFLAQ310 KMMIGRCNRA320 GKPVICATQM330 LESMIKKPRP 340 TRAEGSDVAN350 AVLDGADCIM360 LSGETAKGDY370 PLEAVRMQNL380 IAREAEAAIY 390 HLQLFEELRR400 LAPDPTEATA413 VGAVEASFKC423 CSGAIIVLTK433 SGRSAHQVAR 443 YRPRAPIIAV453 TRNPQTARQA463 HLYRGIFPVL473 CKDPVQEAWA483 EDVDLRVNFA 493 MNVGKARGFF503 KKGDVVIVLT513 GWRPGSGFTN523 TMRVVPVP
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor. Biochem J. 2018 May 31;475(10):1821-1837. | ||||
| REF 2 | M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):5881-6. | ||||
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