eF-site ID 5tbi-B PDB Code 5tbi Chain B click to enlarge Title Crystal structure of mouse CARM1 in complex with inhibitor LH1427 Classification TRANSFERASE Compound Histone-arginine methyltransferase CARM1 Source (CARM1_MOUSE) Sequence B:  RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQ RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV EASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDI IISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVH LAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIP FKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLT HWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIV AQVDQTGSKSSNLLDLKNPFFRY Description Functional site 1) chain B residue 136 type sequence S description binding site for residue PE8 B 501 source : AC7 2) chain B residue 240 type sequence P description binding site for residue PE8 B 501 source : AC7 3) chain B residue 244 type sequence E description binding site for residue PE8 B 501 source : AC7 4) chain B residue 245 type sequence E description binding site for residue PE8 B 501 source : AC7 5) chain B residue 251 type sequence Q description binding site for residue PE8 B 501 source : AC7 6) chain B residue 279 type sequence Y description binding site for residue PE8 B 501 source : AC7 7) chain B residue 267 type sequence E description binding site for residue EDO B 502 source : AC8 8) chain B residue 404 type sequence W description binding site for residue EDO B 503 source : AC9 9) chain B residue 150 type sequence Y description binding site for residue 78V B 504 source : AD1 10) chain B residue 151 type sequence F description binding site for residue 78V B 504 source : AD1 11) chain B residue 154 type sequence Y description binding site for residue 78V B 504 source : AD1 12) chain B residue 163 type sequence M description binding site for residue 78V B 504 source : AD1 13) chain B residue 193 type sequence G description binding site for residue 78V B 504 source : AD1 14) chain B residue 215 type sequence E description binding site for residue 78V B 504 source : AD1 15) chain B residue 216 type sequence A description binding site for residue 78V B 504 source : AD1 16) chain B residue 241 type sequence G description binding site for residue 78V B 504 source : AD1 17) chain B residue 242 type sequence K description binding site for residue 78V B 504 source : AD1 18) chain B residue 243 type sequence V description binding site for residue 78V B 504 source : AD1 19) chain B residue 244 type sequence E description binding site for residue 78V B 504 source : AD1 20) chain B residue 258 type sequence E description binding site for residue 78V B 504 source : AD1 21) chain B residue 260 type sequence M description binding site for residue 78V B 504 source : AD1 22) chain B residue 261 type sequence G description binding site for residue 78V B 504 source : AD1 23) chain B residue 262 type sequence Y description binding site for residue 78V B 504 source : AD1 24) chain B residue 267 type sequence E description binding site for residue 78V B 504 source : AD1 25) chain B residue 269 type sequence M description binding site for residue 78V B 504 source : AD1 26) chain B residue 272 type sequence S description binding site for residue 78V B 504 source : AD1 27) chain B residue 415 type sequence H description binding site for residue 78V B 504 source : AD1 28) chain B residue 416 type sequence W description binding site for residue 78V B 504 source : AD1 29) chain B residue 228 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86X55 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 272 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 160 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 169 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 193 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 215 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 217 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19843527 source Swiss-Prot : SWS_FT_FI2

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