eF-site ID 2v89-ABDE
PDB Code 2v89
Chain A, B, D, E

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Title Crystal structure of RAG2-PHD finger in complex with H3K4me3 peptide at 1.1A resolution
Classification PROTEIN BINDING
Compound VDJ RECOMBINATION-ACTIVATING PROTEIN 2
Source (Q5TEC6_HUMAN)
Sequence A:  SPEFGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHG
DGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARA
B:  GYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHW
VHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARA
D:  ARTXQTAAKA
E:  ARTXQTAAKA
Description


Functional site

1) chain A
residue 1419
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2488
source : AC1

2) chain A
residue 1423
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2488
source : AC1

3) chain A
residue 1455
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2488
source : AC1

4) chain A
residue 1458
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2488
source : AC1

5) chain A
residue 1446
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2489
source : AC2

6) chain A
residue 1452
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2489
source : AC2

7) chain A
residue 1478
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2489
source : AC2

8) chain A
residue 1481
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2489
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 D
residue 3010
type MOD_RES
sequence A
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI8

18) chain E
residue 2010
type MOD_RES
sequence A
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI8

19) chain D
residue 3004
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

20) chain E
residue 2004
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

21) chain D
residue 3005
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

22) chain E
residue 2005
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

23) chain D
residue 3006
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

24) chain E
residue 2006
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

25) chain D
residue 3008
type MOD_RES
sequence A
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

26) chain E
residue 2008
type MOD_RES
sequence A
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

27) chain D
residue 3009
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

28) chain E
residue 2009
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

29) chain D
residue 3002
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

30) chain E
residue 2002
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

31) chain D
residue 3003
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

32) 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

33) 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

34) 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

35) 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

36) 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

37) 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

38) 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

39) chain E
residue 2003
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 1446
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 A
residue 1452
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 1455
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 1458
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 1478
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 1481
type MOD_RES
sequence H
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

46) 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


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