Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T05387 | Target Info | |||
| Target Name | Tissue transglutaminase (TG2) | ||||
| Synonyms | Transglutaminase-2; Transglutaminase H; Transglutaminase C; Transglutaminase 2; Tranglutaminase 2; TTg; TGase-H; TGase-2; TGase H; TGase C; TGC; TG(C)Protein-glutamine gamma-glutamyltransferase; TG(C); Protein-glutamine gamma-glutamyltransferase 2 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | TGM2 | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Adenosine triphosphate | Ligand Info | |||||
| Structure Description | Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate | PDB:3LY6 | ||||
| Method | X-ray diffraction | Resolution | 3.14 Å | Mutation | No | [1] |
| PDB Sequence |
ELVLERCDLE
13 LETNGRDHHT23 ADLCREKLVV33 RRGQPFWLTL43 HFEGRNYEAS53 VDSLTFSVVT 63 GPAPSQEAGT73 KARFPLRDAV83 GDWTATVVDQ95 QDCTLSLQLT105 TPANAPIGLY 115 RLSLEASTGY125 QGSSFVLGHF135 ILLFNAWCPA145 DAVYLDSEEE155 RQEYVLTQQG 165 FIYQGSAKFI175 KNIPWNFGQF185 EDGILDICLI195 LLDVNPKFLK205 NAGRDCSRRS 215 SPVYVGRVGS225 GMVNCNDDQG235 VLLGRWDNNY245 GDGVSPMSWI255 GSVDILRRWK 265 NHGCQRVKYG275 QCWVFAAVAC285 TVLRCLGIPT295 RVVTNYNSAH305 DQNSNLLIEY 315 FRNEFGEIQG325 DKSEMIWNFH335 CWVESWMTRP345 DLQPGYEGWQ355 ALDPTPQEKS 365 EGTYCCGPVP375 VRAIKEGDLS385 TKYDAPFVFA395 EVNADVVDWI405 QQDDGSVHKS 415 INRSLIVGLK425 ISTKSVGRDE435 REDITHTYKY445 PEGSSEEREA455 FTRANHLNKL 465 AEKEETGMAM475 RIRVGQSMNM485 GSDFDVFAHI495 TNNTAEEYVC505 RLLLCARTVS 515 YNGILGPECG525 TKYLLNLNLE535 PFSEKSVPLC545 ILYEKYRDCL555 TESNLIKVRA 565 LLVEPVINSY575 LLAERDLYLE585 NPEIKIRILG595 EPKQKRKLVA605 EVSLQNPLPV 615 ALEGCTFTVE625 GAGLTEEQKT635 VEIPDPVEAG645 EEVKVRMDLL655 PLHMGLHKLV 665 VNFESDKLKA675 VKGFRNVIIG685 PAL
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| Ligand Name: Guanosine-5'-Diphosphate | Ligand Info | |||||
| Structure Description | HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM | PDB:1KV3 | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [2] |
| PDB Sequence |
ETNGRDHHTA
24 DLCREKLVVR34 RGQPFWLTLS56 LTFSVVTGPA66 PSQEAGTKAR76 FPLRDAVEEG 86 DWTATVVDQQ96 DCTLSLQLTT106 PANAPIGLYR116 LSLEASGHFI136 LLFNAWCPAD 146 AVYLDSEEER156 QEYVLTQQGF166 IYQGSAKFIK176 NIPWNFGQFQ186 DGILDICLIL 196 LDVNPKFLKN206 AGRDCSRRSS216 PVYVGRVGSG226 MVNCNDDQGV236 LLGRWDNNYG 246 DGVSPMSWIG256 SVDILRRWKN266 HGCQRVKYGQ276 CWVFAAVACT286 VLRCLGIPTR 296 VVTNYNSAHD306 QNSNLLIEYF316 RNEFGEIQGD326 KSEMIWNFHC336 WVESWMTRPD 346 LQPGYEGWQA356 LDPTPQEKSE366 GTYCCGPVPV376 RAIKEGDLST386 KYDAPFVFAE 396 VNADVVDWIQ406 QDDGSVHKSI416 NRSLIVGLKI426 STKSVGRDER436 EDITHTYKYP 446 EGSSEEREAF456 TRANHLNKLA466 EKEETGMAMR476 IRVGQSMNMG486 SDFDVFAHIT 496 NNTAEEYVCR506 LLLCARTVSY516 NGILGPECGT526 KYLLNLTLEP536 FSEKSVPLCI 546 LYEKYRDCLT556 ESNLIKVRAL566 LVEPVINSYL576 LAERDLYLEN586 PEIKIRILGE 596 PKQKRKLVAE606 VSLQNPLPVA616 LEGCTFTVEG626 AGLTEEQKTV636 EIPDPVEAGE 646 EVKVRMDLVP656 LHMGLHKLVV666 NFESDKLKAV676 KGFRNVIIGP686 A |
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Guanosine-5'-Triphosphate | Ligand Info | |||||
| Structure Description | Transglutaminase 2 mutant G224V in complex with GTP | PDB:6A8P | ||||
| Method | X-ray diffraction | Resolution | 2.54 Å | Mutation | No | [3] |
| PDB Sequence |
MAEELVLERC
10 DLELETNGRD20 HHTADLCREK30 LVVRRGQPFW40 LTLHFEGRNY50 EASVDSLTFS 60 VVTGPAPSQE70 AGTKARFPLR80 DAVEEGDWTA90 TVVDQQDCTL100 SLQLTTPANA 110 PIGLYRLSLE120 ASTGYQGSSF130 VLGHFILLFN140 AWCPADAVYL150 DSEEERQEYV 160 LTQQGFIYQG170 SAKFIKNIPW180 NFGQFEDGIL190 DICLILLDVN200 PKFLKNAGRD 210 CSRRSSPVYV220 GRVVSGMVNC230 NDDQGVLLGR240 WDNNYGDGVS250 PMSWIGSVDI 260 LRRWKNHGCQ270 RVKYGQCWVF280 AAVACTVLRC290 LGIPTRVVTN300 YNSAHDQNSN 310 LLIEYFRNEF320 GEIQGDKSEM330 IWNFHCWVES340 WMTRPDLQPG350 YEGWQALDPT 360 PQEKSEGTYC370 CGPVPVRAIK380 EGDLSTKYDA390 PFVFAEVNAD400 VVDWIQQDDG 410 SVHKSINRSL420 IVGLKISTKS430 VGRDEREDIT440 HTYKYPEGSS450 EEREAFTRAN 460 HLNTGMAMRI477 RVGQSMNMGS487 DFDVFAHITN497 NTAEEYVCRL507 LLCARTVSYN 517 GILGPECGTK527 YLLNLNLEPF537 SEKSVPLCIL547 YEKYRDCLTE557 SNLIKVRALL 567 VEPVINSYLL577 AERDLYLENP587 EIKIRILGEP597 KQKRKLVAEV607 SLQNPLPVAL 617 EGCTFTVEGA627 GLTEEQKTVE637 IPDPVEAGEE647 VKVRMDLLPL657 HMGLHKLVVN 667 FESDKLKAVK677 GFRNVIIGPA687 L
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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 .GTP or .GTP2 or .GTP3 or :3GTP;style chemicals stick;color identity;select .A:173 or .A:174 or .A:476 or .A:477 or .A:478 or .A:479 or .A:480 or .A:481 or .A:482 or .A:483 or .A:580 or .A:581 or .A:582 or .A:583 or .A:584 or .A:585; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol. 2010 Aug 1;47(2):190-5. | ||||
| REF 2 | Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. | ||||
| REF 3 | Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity. PLoS One. 2018 Oct 15;13(10):e0204707. | ||||
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