eF-site ID 5tbi-D
PDB Code 5tbi
Chain D

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Title Crystal structure of mouse CARM1 in complex with inhibitor LH1427
Classification TRANSFERASE
Compound Histone-arginine methyltransferase CARM1
Source (CARM1_MOUSE)
Sequence D:  SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQR
AILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVE
ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDII
ISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHL
APFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPF
KFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTH
WYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVA
QVDQTGSKSSNLLDLKNPFFR
Description


Functional site

1) chain D
residue 458
type
sequence D
description binding site for residue EDO A 501
source : AC1

2) chain D
residue 149
type
sequence Q
description binding site for residue EDO D 501
source : AD9

3) chain D
residue 251
type
sequence Q
description binding site for residue EDO D 502
source : AE1

4) chain D
residue 278
type
sequence K
description binding site for residue EDO D 502
source : AE1

5) chain D
residue 279
type
sequence Y
description binding site for residue EDO D 502
source : AE1

6) chain D
residue 393
type
sequence D
description binding site for residue EDO D 503
source : AE2

7) chain D
residue 150
type
sequence Y
description binding site for residue 78V D 504
source : AE3

8) chain D
residue 151
type
sequence F
description binding site for residue 78V D 504
source : AE3

9) chain D
residue 154
type
sequence Y
description binding site for residue 78V D 504
source : AE3

10) chain D
residue 163
type
sequence M
description binding site for residue 78V D 504
source : AE3

11) chain D
residue 193
type
sequence G
description binding site for residue 78V D 504
source : AE3

12) chain D
residue 215
type
sequence E
description binding site for residue 78V D 504
source : AE3

13) chain D
residue 216
type
sequence A
description binding site for residue 78V D 504
source : AE3

14) chain D
residue 241
type
sequence G
description binding site for residue 78V D 504
source : AE3

15) chain D
residue 242
type
sequence K
description binding site for residue 78V D 504
source : AE3

16) chain D
residue 243
type
sequence V
description binding site for residue 78V D 504
source : AE3

17) chain D
residue 244
type
sequence E
description binding site for residue 78V D 504
source : AE3

18) chain D
residue 258
type
sequence E
description binding site for residue 78V D 504
source : AE3

19) chain D
residue 260
type
sequence M
description binding site for residue 78V D 504
source : AE3

20) chain D
residue 261
type
sequence G
description binding site for residue 78V D 504
source : AE3

21) chain D
residue 262
type
sequence Y
description binding site for residue 78V D 504
source : AE3

22) chain D
residue 267
type
sequence E
description binding site for residue 78V D 504
source : AE3

23) chain D
residue 269
type
sequence M
description binding site for residue 78V D 504
source : AE3

24) chain D
residue 272
type
sequence S
description binding site for residue 78V D 504
source : AE3

25) chain D
residue 415
type
sequence H
description binding site for residue 78V D 504
source : AE3

26) chain D
residue 217
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:19843527
source Swiss-Prot : SWS_FT_FI2

27) chain D
residue 160
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

28) chain D
residue 169
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

29) chain D
residue 193
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

30) chain D
residue 215
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

31) chain D
residue 244
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

32) chain D
residue 272
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17882261
source Swiss-Prot : SWS_FT_FI1

33) 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


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