eF-site ID 5a19-A PDB Code 5a19 Chain A click to enlarge Title The structure of MAT2A in complex with PPNP. Classification TRANSFERASE Compound S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-2 Source Homo sapiens (Human) (METK2_HUMAN) Sequence A:  GTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVA CETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDS SKGFDYKTCNVLVALEQQSPEEDIGAGDQGLMFGYATDET EECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTV QYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKV IKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKI IVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLV KGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELL EIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFP WEVPKKLKY Description Functional site 1) chain A residue 78 type sequence D description BINDING SITE FOR RESIDUE PEG A 400 source : AC1 2) chain A residue 112 type sequence Q description BINDING SITE FOR RESIDUE PEG A 400 source : AC1 3) chain A residue 114 type sequence S description BINDING SITE FOR RESIDUE PEG A 400 source : AC1 4) chain A residue 326 type sequence H description BINDING SITE FOR RESIDUE PEG A 401 source : AC2 5) chain A residue 327 type sequence P description BINDING SITE FOR RESIDUE PEG A 401 source : AC2 6) chain A residue 328 type sequence L description BINDING SITE FOR RESIDUE PEG A 401 source : AC2 7) chain A residue 158 type sequence H description BINDING SITE FOR RESIDUE PEG A 402 source : AC3 8) chain A residue 23 type sequence E description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 9) chain A residue 29 type sequence H description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 10) chain A residue 31 type sequence D description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 11) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 12) chain A residue 181 type sequence K description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 13) chain A residue 258 type sequence D description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 14) chain A residue 264 type sequence R description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 15) chain A residue 265 type sequence K description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 16) chain A residue 280 type sequence G description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 17) chain A residue 281 type sequence A description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 18) chain A residue 285 type sequence K description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 19) chain A residue 291 type sequence D description BINDING SITE FOR RESIDUE PPK A 403 source : AC4 20) chain A residue 36 type sequence Q description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 21) chain A residue 89 type sequence H description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 22) chain A residue 238 type sequence E description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 23) chain A residue 372 type sequence Q description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 24) chain A residue 373 type sequence R description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 25) chain A residue 377 type sequence Y description BINDING SITE FOR RESIDUE PG4 A 407 source : AC5 26) chain A residue 190 type sequence Q description BINDING SITE FOR RESIDUE PEG A 408 source : AC6 27) chain A residue 313 type sequence R description BINDING SITE FOR RESIDUE PEG A 408 source : AC6 28) chain A residue 333 type sequence F description BINDING SITE FOR RESIDUE PEG A 408 source : AC6 29) chain A residue 31 type sequence D description BINDING SITE FOR RESIDUE MG A 409 source : AC7 30) chain A residue 57 type sequence E description BINDING SITE FOR RESIDUE K A 410 source : AC8 31) chain A residue 258 type sequence D description BINDING SITE FOR RESIDUE K A 410 source : AC8 32) chain A residue 259 type sequence A description BINDING SITE FOR RESIDUE K A 410 source : AC8 33) chain A residue 29 type catalytic sequence H description 9 source MCSA : MCSA1 34) chain A residue 264 type catalytic sequence R description 9 source MCSA : MCSA1 35) chain A residue 265 type catalytic sequence K description 9 source MCSA : MCSA1 36) chain A residue 285 type catalytic sequence K description 9 source MCSA : MCSA1 37) chain A residue 289 type catalytic sequence K description 9 source MCSA : MCSA1 38) chain A residue 291 type catalytic sequence D description 9 source MCSA : MCSA1 39) chain A residue 31 type catalytic sequence D description 9 source MCSA : MCSA1 40) chain A residue 32 type catalytic sequence K description 9 source MCSA : MCSA1 41) chain A residue 57 type catalytic sequence E description 9 source MCSA : MCSA1 42) chain A residue 70 type catalytic sequence E description 9 source MCSA : MCSA1 43) chain A residue 181 type catalytic sequence K description 9 source MCSA : MCSA1 44) chain A residue 250 type catalytic sequence F description 9 source MCSA : MCSA1 45) chain A residue 258 type catalytic sequence D description 9 source MCSA : MCSA1 46) chain A residue 259 type catalytic sequence A description 9 source MCSA : MCSA1 47) chain A residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI12 48) chain A residue 57 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P0A817 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 131-141 type prosite sequence GAGDQGLMFGY description ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY source prosite : PS00376 50) chain A residue 278-286 type prosite sequence GGGAFSGKD description ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD source prosite : PS00377 51) chain A residue 29 type BINDING sequence H description in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 264 type BINDING sequence R description in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 285 type BINDING sequence K description BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN source Swiss-Prot : SWS_FT_FI10 54) chain A residue 291 type BINDING sequence D description BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN source Swiss-Prot : SWS_FT_FI10 55) chain A residue 289 type BINDING sequence K description in other chain => ECO:0000250|UniProtKB:P0A817 source Swiss-Prot : SWS_FT_FI11 56) chain A residue 114 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI13 57) chain A residue 384 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 58) chain A residue 228 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI15 59) chain A residue 234 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI15 60) chain A residue 31 type BINDING sequence D description BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I source Swiss-Prot : SWS_FT_FI2 61) chain A residue 70 type BINDING sequence E description in other chain => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN source Swiss-Prot : SWS_FT_FI4 62) chain A residue 113 type BINDING sequence Q description in other chain => ECO:0000305|PubMed:25075345 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 179 type BINDING sequence D description in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I source Swiss-Prot : SWS_FT_FI6 64) chain A residue 247 type BINDING sequence S description in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I source Swiss-Prot : SWS_FT_FI7 65) chain A residue 258 type BINDING sequence D description BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1I source Swiss-Prot : SWS_FT_FI8 66) chain A residue 281 type BINDING sequence A description BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN source Swiss-Prot : SWS_FT_FI9

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