eF-site ID 5k8x-ABCD PDB Code 5k8x Chain A, B, C, D click to enlarge Title Crystal structure of mouse CARM1 in complex with inhibitor U3 Classification TRANSFERASE Compound Histone-arginine methyltransferase CARM1 Source Mus musculus (Mouse) (CARM1_MOUSE) Sequence A:  SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQR AILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVE ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDII ISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHL APFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPF KFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTH WYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVA QVDQTGSKSSNLLDLKNPFFRYT B:  RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQ RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV EASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDI IISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVH LAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIP FKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLT HWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIV AQVDQTGSKSSNLLDLKNPFFRY C:  SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQR AILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVE ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDII ISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHL APFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPF KFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTH WYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVA QVDQTGSKSSNLLDLKNPFFRY D:  RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQ RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV EASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDI IISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVH LAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIP FKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLT HWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIV AQVDQTGSKSSNLLDLKNPFFR Description Functional site 1) chain A residue 150 type sequence Y description binding site for residue 6ZH A 501 source : AC1 2) chain A residue 151 type sequence F description binding site for residue 6ZH A 501 source : AC1 3) chain A residue 154 type sequence Y description binding site for residue 6ZH A 501 source : AC1 4) chain A residue 193 type sequence G description binding site for residue 6ZH A 501 source : AC1 5) chain A residue 215 type sequence E description binding site for residue 6ZH A 501 source : AC1 6) chain A residue 216 type sequence A description binding site for residue 6ZH A 501 source : AC1 7) chain A residue 241 type sequence G description binding site for residue 6ZH A 501 source : AC1 8) chain A residue 242 type sequence K description binding site for residue 6ZH A 501 source : AC1 9) chain A residue 243 type sequence V description binding site for residue 6ZH A 501 source : AC1 10) chain A residue 244 type sequence E description binding site for residue 6ZH A 501 source : AC1 11) chain A residue 258 type sequence E description binding site for residue 6ZH A 501 source : AC1 12) chain A residue 260 type sequence M description binding site for residue 6ZH A 501 source : AC1 13) chain A residue 267 type sequence E description binding site for residue 6ZH A 501 source : AC1 14) chain A residue 269 type sequence M description binding site for residue 6ZH A 501 source : AC1 15) chain A residue 272 type sequence S description binding site for residue 6ZH A 501 source : AC1 16) chain A residue 404 type sequence W description binding site for residue EDO A 502 source : AC2 17) chain A residue 413 type sequence L description binding site for residue EDO A 503 source : AC3 18) chain A residue 414 type sequence T description binding site for residue EDO A 503 source : AC3 19) chain A residue 417 type sequence Y description binding site for residue EDO A 503 source : AC3 20) chain A residue 153 type sequence F description binding site for residue EDO A 504 source : AC4 21) chain A residue 159 type sequence Q description binding site for residue EDO A 504 source : AC4 22) chain A residue 144 type sequence E description binding site for residue EDO A 505 source : AC5 23) chain A residue 242 type sequence K description binding site for residue EDO A 505 source : AC5 24) chain A residue 283 type sequence S description binding site for residue PEG A 506 source : AC6 25) chain A residue 398 type sequence G description binding site for residue PEG A 506 source : AC6 26) chain A residue 399 type sequence S description binding site for residue PEG A 506 source : AC6 27) chain A residue 277 type sequence K description binding site for residue PEG A 507 source : AC7 28) chain A residue 280 type sequence L description binding site for residue PEG A 507 source : AC7 29) chain A residue 282 type sequence P description binding site for residue PEG A 507 source : AC7 30) chain A residue 153 type sequence F description binding site for residue PG4 A 508 source : AC8 31) chain A residue 262 type sequence Y description binding site for residue PG4 A 508 source : AC8 32) chain A residue 267 type sequence E description binding site for residue PG4 A 508 source : AC8 33) chain A residue 415 type sequence H description binding site for residue PG4 A 508 source : AC8 34) chain A residue 416 type sequence W description binding site for residue PG4 A 508 source : AC8 35) chain A residue 456 type sequence Q description binding site for residue PE8 A 509 source : AC9 36) chain A residue 463 type sequence K description binding site for residue PE8 A 509 source : AC9 37) chain B residue 136 type sequence S description binding site for residue PE8 A 509 source : AC9 38) chain B residue 244 type sequence E description binding site for residue PE8 A 509 source : AC9 39) chain B residue 245 type sequence E description binding site for residue PE8 A 509 source : AC9 40) chain B residue 247 type sequence S description binding site for residue PE8 A 509 source : AC9 41) chain B residue 251 type sequence Q description binding site for residue PE8 A 509 source : AC9 42) chain B residue 279 type sequence Y description binding site for residue PE8 A 509 source : AC9 43) chain B residue 150 type sequence Y description binding site for residue 6ZH B 501 source : AD1 44) chain B residue 151 type sequence F description binding site for residue 6ZH B 501 source : AD1 45) chain B residue 154 type sequence Y description binding site for residue 6ZH B 501 source : AD1 46) chain B residue 193 type sequence G description binding site for residue 6ZH B 501 source : AD1 47) chain B residue 215 type sequence E description binding site for residue 6ZH B 501 source : AD1 48) chain B residue 216 type sequence A description binding site for residue 6ZH B 501 source : AD1 49) chain B residue 241 type sequence G description binding site for residue 6ZH B 501 source : AD1 50) chain B residue 242 type sequence K description binding site for residue 6ZH B 501 source : AD1 51) chain B residue 243 type sequence V description binding site for residue 6ZH B 501 source : AD1 52) chain B residue 244 type sequence E description binding site for residue 6ZH B 501 source : AD1 53) chain B residue 258 type sequence E description binding site for residue 6ZH B 501 source : AD1 54) chain B residue 267 type sequence E description binding site for residue 6ZH B 501 source : AD1 55) chain B residue 269 type sequence M description binding site for residue 6ZH B 501 source : AD1 56) chain B residue 272 type sequence S description binding site for residue 6ZH B 501 source : AD1 57) chain B residue 147 type sequence A description binding site for residue EDO B 502 source : AD2 58) chain B residue 242 type sequence K description binding site for residue EDO B 502 source : AD2 59) chain B residue 458 type sequence D description binding site for residue EDO B 503 source : AD3 60) chain C residue 178 type sequence L description binding site for residue EDO B 503 source : AD3 61) chain C residue 205 type sequence Q description binding site for residue EDO B 503 source : AD3 62) chain B residue 415 type sequence H description binding site for residue EDO B 504 source : AD4 63) chain B residue 267 type sequence E description binding site for residue DXE B 506 source : AD5 64) chain C residue 150 type sequence Y description binding site for residue 6ZH C 501 source : AD6 65) chain C residue 151 type sequence F description binding site for residue 6ZH C 501 source : AD6 66) chain C residue 154 type sequence Y description binding site for residue 6ZH C 501 source : AD6 67) chain C residue 193 type sequence G description binding site for residue 6ZH C 501 source : AD6 68) chain C residue 215 type sequence E description binding site for residue 6ZH C 501 source : AD6 69) chain C residue 216 type sequence A description binding site for residue 6ZH C 501 source : AD6 70) chain C residue 241 type sequence G description binding site for residue 6ZH C 501 source : AD6 71) chain C residue 242 type sequence K description binding site for residue 6ZH C 501 source : AD6 72) chain C residue 243 type sequence V description binding site for residue 6ZH C 501 source : AD6 73) chain C residue 244 type sequence E description binding site for residue 6ZH C 501 source : AD6 74) chain C residue 258 type sequence E description binding site for residue 6ZH C 501 source : AD6 75) chain C residue 260 type sequence M description binding site for residue 6ZH C 501 source : AD6 76) chain C residue 267 type sequence E description binding site for residue 6ZH C 501 source : AD6 77) chain C residue 269 type sequence M description binding site for residue 6ZH C 501 source : AD6 78) chain C residue 272 type sequence S description binding site for residue 6ZH C 501 source : AD6 79) chain C residue 410 type sequence T description binding site for residue EDO C 502 source : AD7 80) chain C residue 284 type sequence G description binding site for residue PEG C 504 source : AD8 81) chain C residue 398 type sequence G description binding site for residue PEG C 504 source : AD8 82) chain C residue 399 type sequence S description binding site for residue PEG C 504 source : AD8 83) chain C residue 333 type sequence D description binding site for residue PEG C 505 source : AD9 84) chain C residue 424 type sequence Q description binding site for residue PEG C 505 source : AD9 85) chain C residue 404 type sequence W description binding site for residue PEG C 506 source : AE1 86) chain C residue 277 type sequence K description binding site for residue DXE C 507 source : AE2 87) chain C residue 280 type sequence L description binding site for residue DXE C 507 source : AE2 88) chain C residue 282 type sequence P description binding site for residue DXE C 507 source : AE2 89) chain C residue 361 type sequence L description binding site for residue DXE C 507 source : AE2 90) chain B residue 428 type sequence F description binding site for residue DXE C 508 source : AE3 91) chain C residue 165 type sequence Q description binding site for residue DXE C 508 source : AE3 92) chain D residue 316 type sequence Q description binding site for residue DXE C 508 source : AE3 93) chain C residue 153 type sequence F description binding site for residue DXE C 509 source : AE4 94) chain C residue 159 type sequence Q description binding site for residue DXE C 509 source : AE4 95) chain D residue 472 type sequence N description binding site for residue DXE C 509 source : AE4 96) chain C residue 262 type sequence Y description binding site for residue M2M C 510 source : AE5 97) chain C residue 267 type sequence E description binding site for residue M2M C 510 source : AE5 98) chain D residue 150 type sequence Y description binding site for residue 6ZH D 501 source : AE6 99) chain D residue 151 type sequence F description binding site for residue 6ZH D 501 source : AE6 100) chain D residue 154 type sequence Y description binding site for residue 6ZH D 501 source : AE6 101) chain D residue 193 type sequence G description binding site for residue 6ZH D 501 source : AE6 102) chain D residue 215 type sequence E description binding site for residue 6ZH D 501 source : AE6 103) chain D residue 216 type sequence A description binding site for residue 6ZH D 501 source : AE6 104) chain D residue 241 type sequence G description binding site for residue 6ZH D 501 source : AE6 105) chain D residue 242 type sequence K description binding site for residue 6ZH D 501 source : AE6 106) chain D residue 243 type sequence V description binding site for residue 6ZH D 501 source : AE6 107) chain D residue 244 type sequence E description binding site for residue 6ZH D 501 source : AE6 108) chain D residue 258 type sequence E description binding site for residue 6ZH D 501 source : AE6 109) chain D residue 260 type sequence M description binding site for residue 6ZH D 501 source : AE6 110) chain D residue 267 type sequence E description binding site for residue 6ZH D 501 source : AE6 111) chain D residue 269 type sequence M description binding site for residue 6ZH D 501 source : AE6 112) chain D residue 272 type sequence S description binding site for residue 6ZH D 501 source : AE6 113) chain D residue 404 type sequence W description binding site for residue EDO D 502 source : AE7 114) chain D residue 409 type sequence P description binding site for residue EDO D 505 source : AE9 115) chain D residue 410 type sequence T description binding site for residue EDO D 505 source : AE9 116) chain D residue 411 type sequence E description binding site for residue EDO D 505 source : AE9 117) chain D residue 162 type sequence N description binding site for residue DXE D 507 source : AF1 118) chain D residue 415 type sequence H description binding site for residue DXE D 507 source : AF1 119) chain A 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 120) 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 121) chain C 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 122) chain D 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 123) chain D residue 193 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 124) chain D residue 215 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 125) chain D residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 126) chain D residue 272 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 127) chain B residue 169 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 128) chain B residue 193 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 129) chain A residue 160 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 130) chain A residue 169 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 131) chain A residue 193 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 132) chain A residue 215 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 133) chain A residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 134) chain A residue 272 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 135) chain B residue 160 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 136) chain B residue 215 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 137) chain B residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 138) chain B residue 272 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 139) chain C residue 160 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 140) chain C residue 169 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 141) chain C residue 193 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 142) chain C residue 215 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 143) chain C residue 244 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 144) chain C residue 272 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 160 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 146) chain D residue 169 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17882261 source Swiss-Prot : SWS_FT_FI1 147) chain A residue 217 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19843527 source Swiss-Prot : SWS_FT_FI2 148) chain B residue 217 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19843527 source Swiss-Prot : SWS_FT_FI2 149) chain C residue 217 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19843527 source Swiss-Prot : SWS_FT_FI2 150) chain D residue 217 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19843527 source Swiss-Prot : SWS_FT_FI2

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