eF-site ID 2b3u-AB PDB Code 2b3u Chain A, B click to enlarge Title Human Spermine spermidine acetyltransferase K26R mutant Classification TRANSFERASE Compound Diamine acetyltransferase 1 Source (SAT1_HUMAN) Sequence A:  AKFVIRPATAADCSDILRLIKELAQVILTEKDLLEDGFGE HPFYHCLVAEVPKEHWTPEGHSIVGFAXYYFTYDPWIGKL LYLEDFFVXSDYRGFGIGSEILKNLSQVAXRCRCSSXHFL VAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKXA TE B:  FVIRPATAADCSDILRLIKELARYEYXEEQVILTEKDLLE DGFPFYHCLVAEVPKEHWTPEGHSIVGFAXYYFTYDPWIG KLLYLEDFFVXSDYRGFGIGSEILKNLSQVAXRCRCSSXH FLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLK XATE Description (1)  Diamine acetyltransferase 1 (E.C.2.3.1.57) Functional site 1) chain B residue 142 type sequence R description BINDING SITE FOR RESIDUE SO4 B 172 source : AC1 2) chain B residue 143 type sequence R description BINDING SITE FOR RESIDUE SO4 B 172 source : AC1 3) chain A residue 142 type sequence R description BINDING SITE FOR RESIDUE SO4 A 172 source : AC2 4) chain A residue 143 type sequence R description BINDING SITE FOR RESIDUE SO4 A 172 source : AC2 5) chain B residue 92 type BINDING sequence E description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 94 type BINDING sequence F description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 102 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 133 type BINDING sequence N description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 140 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 152 type BINDING sequence E description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 92 type BINDING sequence E description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 94 type BINDING sequence F description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 102 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 133 type BINDING sequence N description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 140 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 152 type BINDING sequence E description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 27 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17516632 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 140 type ACT_SITE sequence Y description Proton donor => ECO:0000250|UniProtKB:P0A951 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 140 type ACT_SITE sequence Y description Proton donor => ECO:0000250|UniProtKB:P0A951 source Swiss-Prot : SWS_FT_FI1

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