Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T53585 | Target Info | |||
| Target Name | HMG-CoA reductase (HMGCR) | ||||
| Synonyms | 3-hydroxy-3-methylglutaryl-coenzyme A reductase | ||||
| Target Type | Successful Target | ||||
| Gene Name | HMGCR | ||||
| Biochemical Class | CH-OH donor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | adenosine diphosphate | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N | ||||
| InChI | 1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 | ||||
| InChIKey | XTWYTFMLZFPYCI-KQYNXXCUSA-N | ||||
| PubChem Compound ID | 6022 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 1HWL COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ROSUVASTATIN (FORMALLY KNOWN AS ZD4522) | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [1] |
| PDB Sequence |
PRPNEECFLS
463 DAEIIQLVNA473 KHIPAYKLET483 LIETHERGVS493 IRRQLLSKKL503 SEPSSLQYLP 513 YRDYNYSLVM523 GACCENVIGY533 MPIPVGVAGP543 LCLDEKEFQV553 PMATTEGCLV 563 ASTNRGCRAI573 GLGGGASSRV583 LADGMTRGPV593 VRLPRACDSA603 EVKAWLETSE 613 GFAVIKEAFD623 STSRFARLQK633 LHTSIAGRNL643 YIRFQSRSGD653 AMGMNMISKG 663 TEKALSKLHE673 YFPEMQILAV683 SGNYCTDKKP693 AAINWIEGRG703 KSVVCEAVIP 713 AKVVREVLKT723 TTEAMIEVNI733 NKNLVGSAMA743 GSIGGYNAHA753 ANIVTAIYIA 763 CGQDAAQNVG773 SSNCITLMEA783 SGPTNEDLYI793 SCTMPSIEIG803 TVGGGTNLLP 813 QQACLQMLGV823 QGACKDNPGE833 NARQLARIVC843 GTVMAGELSL853 MAALAAG |
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| PDB ID: 1HWK COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ATORVASTATIN | ||||||
| Method | X-ray diffraction | Resolution | 2.22 Å | Mutation | Yes | [1] |
| PDB Sequence |
PRPNEECLLS
463 DAEIIQLVNA473 KHIPAYKLET483 LIETHERGVS493 IRRQLLSKKL503 SEPSSLQYLP 513 YRDYNYSLVM523 GACCENVIGY533 MPIPVGVAGP543 LCLDEKEFQV553 PMATTEGCLV 563 ASTNRGCRAI573 GLGGGASSRV583 LADGMTRGPV593 VRLPRACDSA603 EVKAWLETSE 613 GFAVIKEAFD623 STSRFARLQK633 LHTSIAGRNL643 YIRFQSRSGD653 AMGMNMISKG 663 TEKALSKLHE673 YFPEMQILAV683 SGNYCTDKKP693 AAINWIEGRG703 KSVVCEAVIP 713 AKVVREVLKT723 TTEAMIEVNI733 NKNLVGSAMA743 GSIGGYNAHA753 ANIVTAIYIA 763 CGQDAAQNVG773 SSNCITLMEA783 SGPTNEDLYI793 SCTMPSIEIG803 TVGGGTNLLP 813 QQACLQMLGV823 QGACKDNPGE833 NARQLARIVC843 GTVMAGELSL853 MAALAAGH |
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TYR479
2.934
GLU528
3.843
ASN529
2.937
ALA564
3.644
ASN567
3.379
ARG568
3.407
ARG571
3.812
SER626
4.667
ARG627
4.326
PHE628
3.499
SER651
3.237
GLY652
3.367
ASP653
2.613
ALA654
3.366
MET655
4.120
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| PDB ID: 1HWJ COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH CERIVASTATIN | ||||||
| Method | X-ray diffraction | Resolution | 2.26 Å | Mutation | Yes | [1] |
| PDB Sequence |
PRPNEECLQI
451 LSDAEIIQLV471 NAKHIPAYKL481 ETLIETHERG491 VSIRRQLLSK501 KLSEPSSLQY 511 LPYRDYNYSL521 VMGACCENVI531 GYMPIPVGVA541 GPLCLDEKEF551 QVPMATTEGC 561 LVASTNRGCR571 AIGLGGGASS581 RVLADGMTRG591 PVVRLPRACD601 SAEVKAWLET 611 SEGFAVIKEA621 FDSTSRFARL631 QKLHTSIAGR641 NLYIRFQSRS651 GDAMGMNMIS 661 KGTEKALSKL671 HEYFPEMQIL681 AVSGNYCTDK691 KPAAINWIEG701 RGKSVVCEAV 711 IPAKVVREVL721 KTTTEAMIEV731 NINKNLVGSA741 MAGSIGGYNA751 HAANIVTAIY 761 IACGQDAAQN771 VGSSNCITLM781 EASGPTNEDL791 YISCTMPSIE801 IGTVGGGTNL 811 LPQQACLQML821 GVQGACKDNP831 GENARQLARI841 VCGTVMAGEL851 SLMAALAAGH 861
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| PDB ID: 1HW9 COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH SIMVASTATIN | ||||||
| Method | X-ray diffraction | Resolution | 2.33 Å | Mutation | Yes | [1] |
| PDB Sequence |
PRPNEECKFL
462 SDAEIIQLVN472 AKHIPAYKLE482 TLIETHERGV492 SIRRQLLSKK502 LSEPSSLQYL 512 PYRDYNYSLV522 MGACCENVIG532 YMPIPVGVAG542 PLCLDEKEFQ552 VPMATTEGCL 562 VASTNRGCRA572 IGLGGGASSR582 VLADGMTRGP592 VVRLPRACDS602 AEVKAWLETS 612 EGFAVIKEAF622 DSTSRFARLQ632 KLHTSIAGRN642 LYIRFQSRSG652 DAMGMNMISK 662 GTEKALSKLH672 EYFPEMQILA682 VSGNYCTDKK692 PAAINWIEGR702 GKSVVCEAVI 712 PAKVVREVLK722 TTTEAMIEVN732 INKNLVGSAM742 AGSIGGYNAH752 AANIVTAIYI 762 ACGQDAAQNV772 GSSNCITLME782 ASGPTNEDLY792 ISCTMPSIEI802 GTVGGGTNLL 812 PQQACLQMLG822 VQGACKDNPG832 ENARQLARIV842 CGTVMAGELS852 LMAALAAG |
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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 .ADP or .ADP2 or .ADP3 or :3ADP;style chemicals stick;color identity;select .A:563 or .A:564 or .A:567 or .A:568 or .A:571 or .A:719 or .A:720 or .A:722; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural mechanism for statin inhibition of HMG-CoA reductase. Science. 2001 May 11;292(5519):1160-4. | ||||
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