Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T50594 | Target Info | |||
| Target Name | Serine/threonine-protein kinase pim-1 (PIM1) | ||||
| Synonyms | Pim-1 proto-oncogene, serine/threonine kinase; PIM | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | PIM1 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Cysteine Sulfenic Acid | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)N)SO | ||||
| InChI | 1S/C3H7NO3S/c4-2(1-8-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 | ||||
| InChIKey | FXIRVRPOOYSARH-REOHCLBHSA-N | ||||
| PubChem Compound ID | 165339 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5VUB Pim1 Kinase in complex with a benzofuranone inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
SQYQVGPLLG
45 SGGFGSVYSG55 IRVSDNLPVA65 IKHVEKDRIS75 DWGELPNGTR85 VPMEVVLLKK 95 VSSGFSGVIR105 LLDWFERPDS115 FVLILERPEP125 VQDLFDFITE135 RGALQEELAR 145 SFFWQVLEAV155 RHCHNGVLHR166 DIKDENILID176 LNRGELKLID186 FGSGALLKDT 196 VYTDFDGTRV206 YSPPEWIRYH216 RYHGRSAAVW226 SLGILLYDMV236 CGDIPFEHDE 246 EIIRGQVFFR256 QRVSSECQHL266 IRWCLALRPS276 DRPTFEEIQN286 HPWMQDVLLP 296 QETAEIHLH
|
|||||
|
|
||||||
| PDB ID: 5VUC Pim1 Kinase in complex with a benzofuranone inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
SQYQVGPLLG
45 SGGFGSVYSG55 IRVSDNLPVA65 IKHVEKDRIS75 DWGELPNGTR85 VPMEVVLLKK 95 VSSGFSGVIR105 LLDWFERPDS115 FVLILERPEP125 VQDLFDFITE135 RGALQEELAR 145 SFFWQVLEAV155 RHCHNGVLHR166 DIKDENILID176 LNRGELKLID186 FGSGALLKDT 196 VYTDFDGTRV206 YSPPEWIRYH216 RYHGRSAAVW226 SLGILLYDMV236 CGDIPFEHDE 246 EIIRGQVFFR256 QRVSSECQHL266 IRWCLALRPS276 DRPTFEEIQN286 HPWMQDVLLP 296 QETAEIHLH
|
|||||
|
|
||||||
| PDB ID: 4LM5 Crystal structure of Pim1 in complex with 2-{4-[(3-aminopropyl)amino]quinazolin-2-yl}phenol (resulting from displacement of SKF86002) | ||||||
| Method | X-ray diffraction | Resolution | 2.25 Å | Mutation | No | [2] |
| PDB Sequence |
ESQYQVGPLL
44 GSGGFGSVYS54 GIRVSDNLPV64 AIKHVEKDRI74 SDWGEVPMEV90 VLLKKVSSGF 100 SGVIRLLDWF110 ERPDSFVLIL120 ERPEPVQDLF130 DFITERGALQ140 EELARSFFWQ 150 VLEAVRHCHN160 GVLHRDIKDE171 NILIDLNRGE181 LKLIDFGSGA191 LLKDTVYTDF 201 DGTRVYSPPE211 WIRYHRYHGR221 SAAVWSLGIL231 LYDMVCGDIP241 FEHDEEIIRG 251 QVFFRQRVSS261 ECQHLIRWCL271 ALRPSDRPTF281 EEIQNHPWMQ291 DVLLPQETAE 301 IHLH
|
|||||
|
|
||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Theoretical Analysis of Activity Cliffs among Benzofuranone-Class Pim1 Inhibitors Using the Fragment Molecular Orbital Method with Molecular Mechanics Poisson-Boltzmann Surface Area (FMO+MM-PBSA) Approach. J Chem Inf Model. 2017 Dec 26;57(12):2996-3010. | ||||
| REF 2 | Kinase crystal identification and ATP-competitive inhibitor screening using the fluorescent ligand SKF86002. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):392-404. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.