eF-site ID 1kv3-D PDB Code 1kv3 Chain D 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 D:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA Description Functional site 1) chain D residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 2) chain D residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 3) chain D residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 4) chain D residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 5) chain D residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 6) chain D residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 7) chain D residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 8) chain D residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 9) chain D residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 10) chain D residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 11) chain D residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP D 703 source : AC4 12) chain D residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 13) chain D residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 14) chain D residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 15) chain D residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 16) chain D residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 17) chain D residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 18) chain D residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 19) chain D residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 20) 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 21) chain D residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 22) chain D residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 23) chain D residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 24) 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 25) 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 26) 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

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