eF-site ID 3ep6-AB PDB Code 3ep6 Chain A, B click to enlarge Title Human AdoMetDC D174N mutant complexed with S-Adenosylmethionine methyl ester and no putrescine bound Classification LYASE Compound S-adenosylmethionine decarboxylase beta chain Source Homo sapiens (Human) (DCAM_HUMAN) Sequence A:  SMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQ SFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYC MGRMNSDCWYLYTLDFNQTLEILMSELDPAVMDQFYMKDG VTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDG TYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKP GKFVTTLFVNQPQKIEGFKRLDCQSAMFNDYNFVFTSFAK B:  AHFFEGTEKLLEVWFSRGSGDLRTIPRSEWDILLKDVQCS IISVTKTDKQEAYVLSE Description Functional site 1) chain A residue 69 type sequence S description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 2) chain A residue 80 type sequence K description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 3) chain A residue 81 type sequence T description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 4) chain A residue 243 type sequence H description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 5) chain B residue 64 type sequence V description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 6) chain B residue 65 type sequence L description BINDING SITE FOR RESIDUE PYR A 68 source : AC1 7) chain A residue 69 type sequence S description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 8) chain A residue 81 type sequence T description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 9) chain A residue 82 type sequence C description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 10) chain A residue 223 type sequence F description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 11) chain A residue 224 type sequence N description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 12) chain A residue 226 type sequence C description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 13) chain A residue 227 type sequence G description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 14) chain A residue 228 type sequence Y description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 15) chain A residue 229 type sequence S description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 16) chain A residue 244 type sequence I description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 17) chain A residue 245 type sequence T description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 18) chain A residue 246 type sequence P description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 19) chain A residue 247 type sequence E description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 20) chain B residue 7 type sequence F description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 21) chain B residue 65 type sequence L description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 22) chain B residue 66 type sequence S description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 23) chain B residue 67 type sequence E description BINDING SITE FOR RESIDUE SMM A 368 source : AC2 24) chain A residue 82 type catalytic sequence C description 575 source MCSA : MCSA1 25) chain A residue 229 type catalytic sequence S description 575 source MCSA : MCSA1 26) chain A residue 243 type catalytic sequence H description 575 source MCSA : MCSA1 27) chain A residue 82 type ACT_SITE sequence C description Proton donor; for catalytic activity => ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 11 type ACT_SITE sequence E description Proton donor; for catalytic activity => ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 223 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 247 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 229 type ACT_SITE sequence S description Proton acceptor; for processing activity => ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 243 type ACT_SITE sequence H description Proton acceptor; for processing activity => ECO:0000269|PubMed:11583147 source Swiss-Prot : SWS_FT_FI2

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