eF-site ID 3hl2-D PDB Code 3hl2 Chain D click to enlarge Title The crystal structure of the human SepSecS-tRNASec complex Classification TRANSFERASE Compound O-phosphoseryl-tRNA(Sec) selenium transferase Source Homo sapiens (Human) (3HL2) Sequence D:  EARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMD SNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDIS AVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVVPM ATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITA GFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHS TTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKC MHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSF IQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERK EMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTLDE HRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGF MSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVR K Description Functional site 1) chain D residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 2) chain D residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 3) chain D residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 4) chain D residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 5) chain D residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 6) chain D residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 7) chain D residue 175 type sequence C description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 8) chain D residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 9) chain D residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 10) chain D residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 11) chain D residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 12) chain D residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 13) chain D residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 14) chain D residue 74 type sequence E description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 15) chain D residue 75 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 16) chain D residue 97 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 17) chain D residue 98 type sequence S description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 18) chain D residue 99 type sequence G description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 19) chain D residue 105 type sequence Q description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 20) chain D residue 172 type sequence Q description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 21) chain D residue 173 type sequence K description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 22) chain D residue 284 type sequence K description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 23) chain D residue 313 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 24) chain D residue 199 type sequence R description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 25) chain D residue 234 type sequence R description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 26) chain D residue 368 type sequence H description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 27) chain D residue 74 type SITE sequence E description May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate => ECO:0000250|UniProtKB:Q6P6M7 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 284 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI4

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