eF-site ID 2v83-ABCDE
PDB Code 2v83
Chain A, B, C, D, E

click to enlarge
Title Crystal structure of RAG2-PHD finger in complex with H3K4me3 peptide
Classification PROTEIN BINDING
Compound VDJ RECOMBINATION-ACTIVATING PROTEIN 2
Source (Q5TEC6_HUMAN)
Sequence A:  GYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHW
VHAQCMDLEERTLIHLSEGSNKYYCNEHVQIA
B:  GSPEFGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSH
GDGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARA
C:  GSPEFGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSH
GDGHWVHAQCMDLEERTLIHLSNKYYCNEHVQ
D:  ARTXQTARK
E:  ARTXQTARK
Description (1)  VDJ RECOMBINATION-ACTIVATING PROTEIN 2, HISTONE H3


Functional site

1) chain A
residue 419
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1486
source : AC1

2) chain A
residue 423
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1486
source : AC1

3) chain A
residue 455
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1486
source : AC1

4) chain A
residue 458
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1486
source : AC1

5) chain A
residue 446
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1487
source : AC2

6) chain A
residue 452
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1487
source : AC2

7) chain A
residue 478
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1487
source : AC2

8) chain A
residue 481
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1487
source : AC2

9) chain B
residue 419
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1488
source : AC3

10) chain B
residue 423
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1488
source : AC3

11) chain B
residue 455
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1488
source : AC3

12) chain B
residue 458
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1488
source : AC3

13) chain B
residue 446
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1489
source : AC4

14) chain B
residue 452
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1489
source : AC4

15) chain B
residue 478
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1489
source : AC4

16) chain B
residue 481
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1489
source : AC4

17) chain C
residue 419
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1484
source : AC5

18) chain C
residue 423
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1484
source : AC5

19) chain C
residue 455
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1484
source : AC5

20) chain C
residue 458
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1484
source : AC5

21) chain C
residue 446
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1485
source : AC6

22) chain C
residue 452
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1485
source : AC6

23) chain C
residue 478
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1485
source : AC6

24) chain C
residue 481
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1485
source : AC6

25) chain D
residue 3
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

26) chain B
residue 423
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 446
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 452
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 455
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 458
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 478
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 481
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

33) chain C
residue 419
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

34) chain C
residue 423
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

35) chain C
residue 446
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

36) chain E
residue 3
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

37) chain C
residue 452
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

38) chain C
residue 455
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 458
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

40) chain C
residue 478
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

41) chain C
residue 481
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 446
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 452
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 455
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 458
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 478
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 481
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 419
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

49) chain D
residue 9
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI7

50) chain E
residue 9
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI7

51) chain D
residue 5
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

52) chain E
residue 5
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

53) chain D
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

54) chain E
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

55) chain D
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

56) chain E
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

57) chain D
residue 2
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

58) chain E
residue 2
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

59) chain D
residue 4
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI3

60) chain E
residue 4
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links