eF-site ID 3hl2-ABCDE PDB Code 3hl2 Chain A, B, C, D, E click to enlarge Title The crystal structure of the human SepSecS-tRNASec complex Classification TRANSFERASE Compound O-phosphoseryl-tRNA(Sec) selenium transferase Source null (3HL2) Sequence A:  EARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMD SNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDIS AVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVVPM ATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITA GFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHS TTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKC MHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSF IQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERK EMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTLDE HRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGF MSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVR K B:  GCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGD ISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV PMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCI HSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSS KCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKE RKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL DEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKA VRK C:  QGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELA IMDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSG DISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFV VPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSM ITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILC IHSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQS SKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFN DSFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLK ERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKT LDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTF RGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLK AVRKE D:  EARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMD SNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDIS AVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVVPM ATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITA GFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHS TTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKC MHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSF IQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERK EMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTLDE HRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGF MSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVR K E:  GCCCGGAUGAUCCUCAGUGGUCUGGGGUGCAGGCCUGUAG CUGUCUAGCGACAGAGUGGUUCAAUUCCACCUUUCGGGCG CC Description Functional site 1) chain A residue 74 type sequence E description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 2) chain A residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 3) chain A residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 4) chain A residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 5) chain A residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 6) chain A residue 170 type sequence I description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 7) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 8) chain A residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 9) chain A residue 175 type sequence C description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 10) chain A residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 11) chain A residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 12) chain A residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 13) chain A residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 14) chain A residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 15) chain A residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR A 1001 source : AC1 16) chain A residue 97 type sequence R description BINDING SITE FOR RESIDUE TS6 A 3001 source : AC2 17) chain A residue 98 type sequence S description BINDING SITE FOR RESIDUE TS6 A 3001 source : AC2 18) chain A residue 105 type sequence Q description BINDING SITE FOR RESIDUE TS6 A 3001 source : AC2 19) chain A residue 199 type sequence R description BINDING SITE FOR RESIDUE TS6 A 3002 source : AC3 20) chain A residue 368 type sequence H description BINDING SITE FOR RESIDUE TS6 A 3002 source : AC3 21) chain B residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 22) chain B residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 23) chain B residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 24) chain B residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 25) chain B residue 170 type sequence I description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 26) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 27) chain B residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 28) chain B residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 29) chain B residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 30) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 31) chain B residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 32) chain B residue 311 type sequence P description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 33) chain B residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 34) chain B residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR B 1001 source : AC4 35) chain B residue 74 type sequence E description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 36) chain B residue 75 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 37) chain B residue 97 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 38) chain B residue 98 type sequence S description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 39) chain B residue 99 type sequence G description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 40) chain B residue 105 type sequence Q description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 41) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 42) chain B residue 173 type sequence K description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 43) chain B residue 227 type sequence F description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 44) chain B residue 284 type sequence K description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 45) chain B residue 313 type sequence R description BINDING SITE FOR RESIDUE SEP B 2001 source : AC5 46) chain B residue 199 type sequence R description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 47) chain B residue 234 type sequence R description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 48) chain B residue 368 type sequence H description BINDING SITE FOR RESIDUE SEP B 2002 source : AC6 49) chain C residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 50) chain C residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 51) chain C residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 52) chain C residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 53) chain C residue 170 type sequence I description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 54) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 55) chain C residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 56) chain C residue 175 type sequence C description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 57) chain C residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 58) chain C residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 59) chain C residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 60) chain C residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 61) chain C residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 62) chain C residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR C 1001 source : AC7 63) chain C residue 97 type sequence R description BINDING SITE FOR RESIDUE TS6 C 3001 source : AC8 64) chain C residue 98 type sequence S description BINDING SITE FOR RESIDUE TS6 C 3001 source : AC8 65) chain C residue 105 type sequence Q description BINDING SITE FOR RESIDUE TS6 C 3001 source : AC8 66) chain D residue 75 type sequence R description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 67) chain D residue 143 type sequence A description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 68) chain D residue 144 type sequence T description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 69) chain D residue 145 type sequence G description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 70) chain D residue 172 type sequence Q description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 71) chain D residue 174 type sequence S description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 72) chain D residue 175 type sequence C description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 73) chain D residue 252 type sequence N description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 74) chain D residue 254 type sequence A description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 75) chain D residue 255 type sequence Y description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 76) chain D residue 284 type sequence K description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 77) chain D residue 312 type sequence G description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 78) chain D residue 313 type sequence R description BINDING SITE FOR RESIDUE PLR D 1001 source : AC9 79) chain D residue 74 type sequence E description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 80) chain D residue 75 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 81) chain D residue 97 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 82) chain D residue 98 type sequence S description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 83) chain D residue 99 type sequence G description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 84) chain D residue 105 type sequence Q description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 85) chain D residue 172 type sequence Q description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 86) chain D residue 173 type sequence K description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 87) chain D residue 284 type sequence K description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 88) chain D residue 313 type sequence R description BINDING SITE FOR RESIDUE SEP D 2001 source : BC1 89) chain D residue 199 type sequence R description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 90) chain D residue 234 type sequence R description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 91) chain D residue 368 type sequence H description BINDING SITE FOR RESIDUE SEP D 2002 source : BC2 92) chain B residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 93) chain B residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 94) chain B residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 95) chain B residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 96) chain B residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 98) chain B residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 99) chain C residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 100) chain C residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 101) chain C residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 102) chain C residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 103) chain C residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 104) chain C residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 105) chain C residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 106) chain C residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 107) chain D residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 108) chain D residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 109) chain D residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 110) chain D residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 111) chain D residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 112) chain D residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 113) chain D residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 114) chain D residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 115) chain A residue 271 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 116) chain A residue 313 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 117) chain A residue 398 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 118) chain A residue 463 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 119) chain B residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 120) chain A residue 97 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 121) chain A residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 122) chain A residue 105 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 123) chain A residue 75 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI1 124) chain A 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 125) 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 126) chain C 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 127) 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 128) chain A residue 124-134 type prosite sequence DIIKLAGVHTV description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIIKLAGVHTV source prosite : PS00435 129) chain B residue 284 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI4 130) chain C residue 284 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI4 131) chain D residue 284 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919 source Swiss-Prot : SWS_FT_FI4 132) chain A 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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