eF-site ID 3hl2-B PDB Code 3hl2 Chain B 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 B:  GCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGD ISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV PMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCI HSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSS KCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKE RKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL DEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKA VRK Description Functional site 1) chain B residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 2) chain B residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 3) chain B residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 4) chain B residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 5) chain B residue 170 type sequence I description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 6) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 7) chain B residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 8) chain B residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 9) chain B residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 10) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 11) chain B residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 12) chain B residue 311 type sequence P description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 13) chain B residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 14) chain B residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 15) chain B residue 74 type sequence E description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 16) chain B residue 75 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 17) chain B residue 97 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 18) chain B residue 98 type sequence S description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 19) chain B residue 99 type sequence G description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 20) chain B residue 105 type sequence Q description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 21) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 22) chain B residue 173 type sequence K description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 23) chain B residue 227 type sequence F description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 24) chain B residue 284 type sequence K description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 25) chain B residue 313 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 26) chain B residue 199 type sequence R description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 27) chain B residue 234 type sequence R description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 28) chain B residue 368 type sequence H description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 29) chain B 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 30) chain B residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 38) chain B 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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