eF-site ID 1kv3-ABCDEF PDB Code 1kv3 Chain A, B, C, D, E, F click to enlarge Title HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM Classification TRANSFERASE Compound Protein-glutamine gamma-glutamyltransferase Source Homo sapiens (Human) (TGM2_HUMAN) Sequence A:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA B:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA C:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA D:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA E:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA F:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA Description Functional site 1) chain A residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 2) chain A residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 3) chain A residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 4) chain A residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 5) chain A residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 6) chain A residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 7) chain A residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 8) chain A residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 9) chain A residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 10) chain A residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 11) chain A residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP A 700 source : AC1 12) chain B residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 13) chain B residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 14) chain B residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 15) chain B residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 16) chain B residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 17) chain B residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 18) chain B residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 19) chain B residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 20) chain B residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 21) chain B residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 22) chain B residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP B 701 source : AC2 23) chain C residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 24) chain C residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 25) chain C residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 26) chain C residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 27) chain C residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 28) chain C residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 29) chain C residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 30) chain C residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 31) chain C residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 32) chain C residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 33) chain C residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 34) chain D residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 35) chain D residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 36) chain D residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 37) chain D residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 38) chain D residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 39) chain D residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 40) chain D residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 41) chain D residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 42) chain D residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 43) chain D residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 44) chain D residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 45) chain E residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 46) chain E residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 47) chain E residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 48) chain E residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 49) chain E residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 50) chain E residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 51) chain E residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 52) chain E residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 53) chain E residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 54) chain E residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 55) chain E residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP E 704 source : AC5 56) chain F residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 57) chain F residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 58) chain F residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 59) chain F residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 60) chain F residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 61) chain F residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 62) chain F residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 63) chain F residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 64) chain F residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 65) chain F residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 66) chain F residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP F 705 source : AC6 67) chain A residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 68) chain E residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 69) chain F residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 70) chain F residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 74) chain C residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 75) chain C residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 76) chain D residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 77) chain D residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 78) chain E residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 79) chain A residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 80) chain C residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 81) chain C residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 82) chain C residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 83) chain D residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 84) chain D residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 85) chain D residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 86) chain D residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 87) chain E residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 88) chain E residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 89) chain E residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 90) chain A residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 91) chain E residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 92) chain F residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 93) chain F residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 94) chain F residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 95) chain F residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 96) chain A residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 97) chain A residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 98) chain B residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 99) chain B residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 100) chain B residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 101) chain B residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 102) chain C residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 103) chain A residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 104) chain E residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 105) chain F residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 106) chain F residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 107) chain A residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 108) chain B residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 109) chain B residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 110) chain C residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 111) chain C residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 112) chain D residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 113) chain D residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 114) chain E residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 115) chain A residue 275-292 type prosite sequence GQCWVFAAVACTVLRCLG description TRANSGLUTAMINASES Transglutaminases active site. GQCWVfAAVacTvLRCLG source prosite : PS00547 116) chain A residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 117) chain F residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 118) chain B residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 119) chain C residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 120) chain D residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 121) chain E residue 633 type CROSSLNK sequence Q description Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) => ECO:0000250|UniProtKB:P08587 source Swiss-Prot : SWS_FT_FI10 122) chain A residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 123) chain B residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 124) chain C residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 125) chain D residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 126) chain E residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 127) chain F residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 128) chain A residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 129) chain B residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 130) chain C residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 131) chain D residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 132) chain E residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 133) chain F residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 134) chain A residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 135) chain B residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 136) chain C residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 137) chain D residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 138) chain E residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 139) chain F residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 140) chain A residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 141) chain B residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 142) chain C residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 143) chain D residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 144) chain E residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 145) chain F residue 277 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000305|PubMed:7649299, ECO:0000305|PubMed:8943303 source Swiss-Prot : SWS_FT_FI1 146) chain A residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 147) chain E residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 148) chain F residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 149) chain F residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 150) chain A residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 151) chain B residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 152) chain B residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 153) chain C residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 154) chain C residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 155) chain D residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 156) chain D residue 580 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5 157) chain E residue 476 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:30321187, ECO:0000269|PubMed:31991788, ECO:0000305|PubMed:11867708, ECO:0000305|PubMed:20450932, ECO:0007744|PDB:1KV3, ECO:0007744|PDB:3LY6, ECO:0007744|PDB:4PYG, ECO:0007744|PDB:6A8P, ECO:0007744|PDB:6KZB source Swiss-Prot : SWS_FT_FI5

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