Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T17986 | Target Info | |||
| Target Name | Enhancer of zeste homolog 1 (EZH1) | ||||
| Synonyms | KIAA0388; Histone-lysine N-methyltransferase EZH1; ENX-2 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | EZH1 | ||||
| Biochemical Class | Methyltransferase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Ademetionine | Ligand Info | |||||
| Structure Description | Structure of human PRC2-EZH1 containing phosphorylated SUZ12 | PDB:7TD5 | ||||
| Method | X-ray diffraction | Resolution | 2.99 Å | Mutation | No | [1] |
| PDB Sequence |
SEYMRLRQLK
30 RLQANMGAKA40 LYVANFAKVQ50 EKTQILNEEW60 KKLRVQPVQS70 MLKKCTIESI 88 FPGFASQHML98 MRSLNTVALV108 PIMYSWSPLQ118 QNFMVEDETV128 LCNIPYMGDE 138 VKEEDETFIE148 ELINNYDGKV158 HGEEQCTPNI277 DGPNAKSVQR287 EQSLHSFHTL 297 FCRRCFKYDC307 FLHPFHATPN317 VYKRKNKEIK327 IEPEPCGTDC337 FLLLEGAKEY 347 AMLHNVEAPS429 PVEWTGAEES440 LFRVFHGTYF450 NNFCSIARLL460 GTKTCKQVFQ 470 FAVKESLILS515 TQVYNYQPCD525 HPDRPCDSTC535 PCIMTQNFCE545 KFCQCNPDCQ 555 NRFPGCRCKT565 QCNTKQCPCY575 LAVRECDPDL585 CLTCGASEHW595 DCKVVSCKNC 605 SIQRGLKKHL615 LLAPSDVAGW625 GTFIKESVQK635 NEFISEYCGE645 LISQDEADRR 655 GKVYDKYMSS665 FLFNLNNDFV675 VDATRKGNKI685 RFANHSVNPN695 CYAKVVMVNG 705 DHRIGIFAKR715 AIQAGEELFF725 DYRYSQADAL735 KYVGIER
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ILE110
4.466
VAL622
3.617
ALA623
2.976
GLY624
3.439
TRP625
2.786
TYR642
4.346
MET663
2.732
SER664
3.592
SER665
3.293
PHE666
3.438
ARG686
3.194
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| Ligand Name: L-serine-O-phosphate | Ligand Info | |||||
| Structure Description | Structure of human PRC2-EZH1 containing phosphorylated SUZ12 | PDB:7TD5 | ||||
| Method | X-ray diffraction | Resolution | 2.99 Å | Mutation | No | [1] |
| PDB Sequence |
SEYMRLRQLK
30 RLQANMGAKA40 LYVANFAKVQ50 EKTQILNEEW60 KKLRVQPVQS70 MLKKCTIESI 88 FPGFASQHML98 MRSLNTVALV108 PIMYSWSPLQ118 QNFMVEDETV128 LCNIPYMGDE 138 VKEEDETFIE148 ELINNYDGKV158 HGEEQCTPNI277 DGPNAKSVQR287 EQSLHSFHTL 297 FCRRCFKYDC307 FLHPFHATPN317 VYKRKNKEIK327 IEPEPCGTDC337 FLLLEGAKEY 347 AMLHNVEAPS429 PVEWTGAEES440 LFRVFHGTYF450 NNFCSIARLL460 GTKTCKQVFQ 470 FAVKESLILS515 TQVYNYQPCD525 HPDRPCDSTC535 PCIMTQNFCE545 KFCQCNPDCQ 555 NRFPGCRCKT565 QCNTKQCPCY575 LAVRECDPDL585 CLTCGASEHW595 DCKVVSCKNC 605 SIQRGLKKHL615 LLAPSDVAGW625 GTFIKESVQK635 NEFISEYCGE645 LISQDEADRR 655 GKVYDKYMSS665 FLFNLNNDFV675 VDATRKGNKI685 RFANHSVNPN695 CYAKVVMVNG 705 DHRIGIFAKR715 AIQAGEELFF725 DYRYSQADAL735 KYVGIER
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| Ligand Name: N-Trimethyllysine | Ligand Info | |||||
| Structure Description | Structure of human PRC2-EZH1 containing phosphorylated SUZ12 | PDB:7TD5 | ||||
| Method | X-ray diffraction | Resolution | 2.99 Å | Mutation | No | [1] |
| PDB Sequence |
SEYMRLRQLK
30 RLQANMGAKA40 LYVANFAKVQ50 EKTQILNEEW60 KKLRVQPVQS70 MLKKCTIESI 88 FPGFASQHML98 MRSLNTVALV108 PIMYSWSPLQ118 QNFMVEDETV128 LCNIPYMGDE 138 VKEEDETFIE148 ELINNYDGKV158 HGEEQCTPNI277 DGPNAKSVQR287 EQSLHSFHTL 297 FCRRCFKYDC307 FLHPFHATPN317 VYKRKNKEIK327 IEPEPCGTDC337 FLLLEGAKEY 347 AMLHNVEAPS429 PVEWTGAEES440 LFRVFHGTYF450 NNFCSIARLL460 GTKTCKQVFQ 470 FAVKESLILS515 TQVYNYQPCD525 HPDRPCDSTC535 PCIMTQNFCE545 KFCQCNPDCQ 555 NRFPGCRCKT565 QCNTKQCPCY575 LAVRECDPDL585 CLTCGASEHW595 DCKVVSCKNC 605 SIQRGLKKHL615 LLAPSDVAGW625 GTFIKESVQK635 NEFISEYCGE645 LISQDEADRR 655 GKVYDKYMSS665 FLFNLNNDFV675 VDATRKGNKI685 RFANHSVNPN695 CYAKVVMVNG 705 DHRIGIFAKR715 AIQAGEELFF725 DYRYSQADAL735 KYVGIER
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .M3L or .M3L2 or .M3L3 or :3M3L;style chemicals stick;color identity;select .A:134 or .A:137; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site. Nat Commun. 2022 Nov 9;13(1):6781. | ||||
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