eF-site ID 1boi-A PDB Code 1boi Chain A click to enlarge Title N-TERMINALLY TRUNCATED RHODANESE Classification TRANSFERASE Compound RHODANESE Source null (THTR_BOVIN) Sequence A:  ALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEY LERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSL GISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLN GGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQV LENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGS VNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATX RKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETW VSQGKG Description (1)  RHODANESE Functional site 1) chain A residue 71 type sequence E description AT THE CATION-BINDING SITE A SMALL ION (NA+ OR K+) IS BOUND. source : CT1 2) chain A residue 72 type sequence V description AT THE CATION-BINDING SITE A SMALL ION (NA+ OR K+) IS BOUND. source : CT1 3) chain A residue 73 type sequence M description AT THE CATION-BINDING SITE A SMALL ION (NA+ OR K+) IS BOUND. source : CT1 4) chain A residue 249 type sequence K description AT THE CATION-BINDING SITE A SMALL ION (NA+ OR K+) IS BOUND. source : CT1 5) chain A residue 272 type sequence D description AT THE CATION-BINDING SITE A SMALL ION (NA+ OR K+) IS BOUND. source : CT1 6) chain A residue 187 type catalytic sequence Y description 153 source MCSA : MCSA1 7) chain A residue 248 type catalytic sequence R description 153 source MCSA : MCSA1 8) chain A residue 249 type catalytic sequence K description 153 source MCSA : MCSA1 9) chain A residue 250 type catalytic sequence G description 153 source MCSA : MCSA1 10) chain A residue 251 type catalytic sequence V description 153 source MCSA : MCSA1 11) chain A residue 252 type catalytic sequence T description 153 source MCSA : MCSA1 12) chain A residue 253 type catalytic sequence A description 153 source MCSA : MCSA1 13) chain A residue 275 type catalytic sequence W description 153 source MCSA : MCSA1 14) chain A residue 35 type CARBOHYD sequence W description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 15) chain A residue 248 type ACT_SITE sequence R description Cysteine persulfide intermediate => ECO:0000255|PROSITE-ProRule:PRU00173, ECO:0000269|PubMed:711738 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 14 type MOD_RES sequence W description N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 38 type MOD_RES sequence P description Phosphoserine => ECO:0000250|UniProtKB:P24329 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 224 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 237 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 136 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 175 type MOD_RES sequence R description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI5 22) chain A residue 236 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI6 23) chain A residue 163 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P52196 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 47-58 type prosite sequence YLERHVPGASFF description RHODANESE_1 Rhodanese signature 1. YlerHVPGAsfF source prosite : PS00380 25) chain A residue 268-278 type prosite sequence VAIYDGSWFEW description RHODANESE_2 Rhodanese C-terminal signature. VaiYDGSWfEW source prosite : PS00683 26) chain A residue 187 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 27) chain A residue 250 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2

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