eF-site ID 1kv3-C PDB Code 1kv3 Chain C 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 C:  ETNGRDHHTADLCREKLVVRRGQPFWLTLSLTFSVVTGPA PSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTT PANAPIGLYRLSLEASGHFILLFNAWCPADAVYLDSEEER QEYVLTQQGFIYQGSAKFIKNIPWNFGQFQDGILDICLIL LDVNPKFLKNAGRDCSRRSSPVYVGRVGSGMVNCNDDQGV LLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQ CWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYF RNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQA LDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAE VNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDER EDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMR IRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSY NGILGPECGTKYLLNLTLEPFSEKSVPLCILYEKYRDCLT ESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGE PKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTV EIPDPVEAGEEVKVRMDLVPLHMGLHKLVVNFESDKLKAV KGFRNVIIGPA Description Functional site 1) chain C residue 174 type sequence F description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 2) chain C residue 476 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 3) chain C residue 478 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 4) chain C residue 479 type sequence V description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 5) chain C residue 480 type sequence G description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 6) chain C residue 481 type sequence Q description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 7) chain C residue 482 type sequence S description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 8) chain C residue 483 type sequence M description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 9) chain C residue 580 type sequence R description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 10) chain C residue 582 type sequence L description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 11) chain C residue 583 type sequence Y description BINDING SITE FOR RESIDUE GDP C 702 source : AC3 12) chain C residue 335 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 358 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 400 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 447 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 452 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 398 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00488 source Swiss-Prot : SWS_FT_FI3 18) chain C residue 437 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 19) chain C residue 539 type BINDING sequence E description BINDING => ECO:0000305|PubMed:31991788 source Swiss-Prot : SWS_FT_FI4 20) 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 21) chain C residue 468 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P21981 source Swiss-Prot : SWS_FT_FI9 22) chain C residue 516 type SITE sequence Y description Important for catalytic activity => ECO:0000250|UniProtKB:P52181 source Swiss-Prot : SWS_FT_FI6 23) chain C residue 60 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 24) 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 25) 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 26) 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

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