eF-site ID 3u0o-AB PDB Code 3u0o Chain A, B click to enlarge Title The crystal structure of selenophosphate synthetase from E. coli Classification TRANSFERASE Compound Selenide, water dikinase Source null (SELD_ECOLI) Sequence A:  ILHSEQAKFVDPNLLVGNETRDDAAVYDLGNGTSVISTTD FFMPIVDNPFDFGRIAATNAISDIFAMGGKPIMAIAILGW PINKLSPEIAREVTEGGRYACRQAGIALAGGHSIDAPEPI FGLAVTGIVPTERVKKNSTAQAGCKLFLTKPLGIGVLTTA EKKSLLKPEHQGLATEVMCRMNIAGASFANIEGVKAMTDV TGFGLLGHLSEMCQGAGVQARVDYEAIPKLPGVEEYIKLG AVPGGTERNFASYGHLMGEMPREVRDLLCDPQTSGGLLLA VMPEAENEVKATAAEFGIELTAIGELVPARGGRAMVEIR B:  HGAGCGCKISPKVLETILHSEQAKFVDPNLLVGNETRDDA AVYDLGNGTSVISTTDFFMPIVDNPFDFGRIAATNAISDI FAMGGKPIMAIAILGWPINKLSPEIAREVTEGGRYACRQA GIALAGGHSIDAPEPIFGLAVTGIVPTERVKKNSTAQAGC KLFLTKPLGIGVLTTAEKKSLLKPEHQGLATEVMCRMNIA GASFANIEGVKAMTDVTGFGLLGHLSEMCQGAGVQARVDY EAIPKLPGVEEYIKLGAVPGGTERNFASYGHLMGEMPREV RDLLCDPQTSGGLLLAVMPEAENEVKATAAEFGIELTAIG ELVPARGGRAMVEIR Description Functional site 1) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE MG A 401 source : AC1 2) chain A residue 91 type sequence D description BINDING SITE FOR RESIDUE MG A 401 source : AC1 3) chain A residue 227 type sequence D description BINDING SITE FOR RESIDUE MG A 401 source : AC1 4) chain B residue 91 type sequence D description BINDING SITE FOR RESIDUE MG B 401 source : AC2 5) chain B residue 227 type sequence D description BINDING SITE FOR RESIDUE MG B 401 source : AC2 6) chain B residue 229 type sequence T description BINDING SITE FOR RESIDUE MG B 401 source : AC2 7) chain B residue 17 type ACT_SITE sequence C description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 68 type BINDING sequence D description in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 20 type BINDING sequence K description in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 48 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 68 type BINDING sequence D description in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 48 type BINDING sequence T description in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 227 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 14) chain B residue 51 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 15) chain B residue 91 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 16) chain B residue 227 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 17) chain A residue 91 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 18) chain A residue 51 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O source Swiss-Prot : SWS_FT_FI3 19) chain B residue 139 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 139 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 20 type SITE sequence K description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:8262938 source Swiss-Prot : SWS_FT_FI5

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