Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T23995 | Target Info | |||
| Target Name | Protein kinase C theta (PRKCQ) | ||||
| Synonyms | Protein kinase C theta type; PRKCT; NPKC-theta | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | PRKCQ | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | L-serine-O-phosphate | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)N)OP(=O)(O)O | ||||
| InChI | 1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 | ||||
| InChIKey | BZQFBWGGLXLEPQ-REOHCLBHSA-N | ||||
| PubChem Compound ID | 68841 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5F9E Structure of Protein Kinase C theta with compound 10: 2,2-dimethyl-7-(2-oxidanylidene-3~{H}-imidazo[4,5-b]pyridin-1-yl)-1-(phenylmethyl)-3~{H}-quinazolin-4-one | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
KLKIEDFELH
383 KMLGKGSFGK393 VFLAEFKKTN403 QFFAIKALKK413 DVVLMDDDVE423 CTMVEKRVLS 433 LAWEHPFLTH443 MFCTFQTKEN453 LFFVMEYLNG463 GDLMYHIQSC473 HKFDLSRATF 483 YAAEIILGLQ493 FLHSKGIVYR503 DLKLDNILLD513 KDGHIKIADF523 GMCKENMLGD 533 AKTNEFCGTP543 DYIAPEILLG553 QKYNHSVDWW563 SFGVLLYEML573 IGQSPFHGQD 583 EEELFHSIRM593 DNPFYPRWLE603 KEAKDLLVKL613 FVREPEKRLG623 VRGDIRQHPL 633 FREINWEELE643 RKEIDPPFRP653 KVKSPFDCSN663 FDKEFLNEKP673 RLFADRALIN 684 SMDQNMFRNF694 FMNPGMERLI705 SHHH
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| PDB ID: 2JED The crystal structure of the kinase domain of the protein kinase C theta in complex with NVP-XAA228 at 2.32A resolution. | ||||||
| Method | X-ray diffraction | Resolution | 2.32 Å | Mutation | Yes | [2] |
| PDB Sequence |
LKIEDFELHK
384 MLGKGSFGKV394 FLAEFKKTNQ404 FFAIKALKKD414 VVLMDDDVEC424 TMVEKRVLSL 434 AWEHPFLTHM444 FCTFQTKENL454 FFVMEYLNGG464 DLMYHIQSCH474 KFDLSRATFY 484 AAEIILGLQF494 LHSKGIVYRD504 LKLDNILLDK514 DGHIKIADFG524 MCKENMLGDA 534 KTNEFCGTPD544 YIAPEILLGQ554 KYNHSVDWWS564 FGVLLYEMLI574 GQSPFHGQDE 584 EELFHSIRMD594 NPFYPRWLEK604 EAKDLLVKLF614 VREPEKRLGV624 RGDIRQHPLF 634 REINWEELER644 KEIDPPFRPK654 VKSPFDCSNF664 DKEFLNEKPR674 LFADRALINS 685 MDQNMFRNFF696 MNPG
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| PDB ID: 1XJD Crystal Structure of PKC-theta complexed with Staurosporine at 2A resolution | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [3] |
| PDB Sequence |
IEDFILHKML
386 GKGSFGKVFL396 AEFKKTNQFF406 AIKALKKDVV416 LMDDDVECTM426 VEKRVLSLAW 436 EHPFLTHMFC446 TFQTKENLFF456 VMEYLNGGDL466 MYHIQSCHKF476 DLSRATFYAA 486 EIILGLQFLH496 SKGIVYRDLK506 LDNILLDKDG516 HIKIADFGMC526 KENMLGDAKT 536 NFCGTPDYIA547 PEILLGQKYN557 HSVDWWSFGV567 LLYEMLIGQS577 PFHGQDEEEL 587 FHSIRMDNPF597 YPRWLEKEAK607 DLLVKLFVRE617 PEKRLGVRGD627 IRQHPLFREI 637 NWEELERKEI647 DPQNMFRNFF696
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| PDB ID: 4Q9Z Human Protein Kinase C Theta in Complex with Compound35 ((1R)-9-(AZETIDIN-3-YLAMINO)-1,8-DIMETHYL-3,5-DIHYDRO[1,2,4]TRIAZINO[3,4-C][1,4]BENZOXAZIN-2(1H)-ONE) | ||||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | Yes | [4] |
| PDB Sequence |
LKIEDFELHK
384 MLGKGSFGKV394 FLAEFKKTNQ404 FFAIKALKKD414 VVLMDDDVEC424 TMVEKRVLSL 434 AWEHPFLTHM444 FCTFQTKENL454 FFVMEYLNGG464 DLMYHIQSCH474 KFDLSRATFY 484 AAEIILGLQF494 LHSKGIVYRD504 LKLDNILLDK514 DGHIKIADFG524 MCKENMLGDA 534 KTNEFCGTPD544 YIAPEILLGQ554 KYNHSVDWWS564 FGVLLYEMLI574 GQSPFHGQDE 584 EELFHSIRMD594 NPFYPRWLEK604 EAKDLLVKLF614 VREPEKRLGV624 RGDIRQHPLF 634 REINWEELER644 KEIDPPFRPK654 VKSPFDCSNF664 DKEFLNEKPR674 LFADRALINS 685 MDQNMFRNFF696 MNPGMERLIS706 H
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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 .SEP or .SEP2 or .SEP3 or :3SEP;style chemicals stick;color identity;select .A:388 or .A:393 or .A:412 or .A:429 or .A:447 or .A:448 or .A:449 or .A:452 or .A:674 or .A:675 or .A:677 or .A:678 or .A:691 or .A:693 or .A:694 or .A:696 or .A:697; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 4RA5 Human Protein Kinase C THETA IN COMPLEX WITH LIGAND COMPOUND 11a (6-[(1,3-Dimethyl-azetidin-3-yl)-methyl-amino]-4(R)-methyl-7-phenyl-2,10-dihydro-9-oxa-1,2,4a-triaza-phenanthren-3-one) | ||||||
| Method | X-ray diffraction | Resolution | 2.61 Å | Mutation | Yes | [5] |
| PDB Sequence |
KLKIEDFELH
383 KMLGKGSFGK393 VFLAEFKKTN403 QFFAIKALKK413 DVVLMDDDVE423 CTMVEKRVLS 433 LAWEHPFLTH443 MFCTFQTKEN453 LFFVMEYLNG463 GDLMYHIQSC473 HKFDLSRATF 483 YAAEIILGLQ493 FLHSKGIVYR503 DLKLDNILLD513 KDGHIKIADF523 GMCKENMLGD 533 AKTNEFCGTP543 DYIAPEILLG553 QKYNHSVDWW563 SFGVLLYEML573 IGQSPFHGQD 583 EEELFHSIRM593 DNPFYPRWLE603 KEAKDLLVKL613 FVREPEKRLG623 VRGDIRQHPL 633 FREINWEELE643 RKEIDPPFRP653 KVKSPFDCSN663 FDKEFLNEKP673 RLFADRALIN 684 SMDQNMFRNF694 FMNPGMERLI705 SH
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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 .SEP or .SEP2 or .SEP3 or :3SEP;style chemicals stick;color identity;select .A:388 or .A:393 or .A:412 or .A:429 or .A:447 or .A:448 or .A:449 or .A:452 or .A:674 or .A:675 or .A:677 or .A:678 or .A:693 or .A:694 or .A:696 or .A:697; 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 | Discovery and optimization of 1,7-disubstituted-2,2-dimethyl-2,3-dihydroquinazolin-4(1H)-ones as potent and selective PKC-Theta inhibitors. Bioorg Med Chem. 2016 Jun 1;24(11):2466-75. | ||||
| REF 2 | The Crystal Structure of the Kinase Domain of the Protein Kinase C Theta in Complex with Nvp-Xaa228 | ||||
| REF 3 | Catalytic domain crystal structure of protein kinase C-theta (PKCtheta). J Biol Chem. 2004 Nov 26;279(48):50401-9. | ||||
| REF 4 | Discovery of selective and orally bioavailable protein kinase C (PKC) inhibitors from a fragment hit. J Med Chem. 2015 Jan 8;58(1):222-36. | ||||
| REF 5 | Optimized protein kinase C-Theta (PKC-Theta) inhibitors reveal only modest anti-inflammatory efficacy in a rodent model of arthritis. J Med Chem. 2015 Jan 8;58(1):333-46. | ||||
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