eF-site ID 2lgg_15-AB
PDB Code 2lgg
Model 15
Chain A, B

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Title Structure of PHD domain of UHRF1 in complex with H3 peptide
Classification LIGASE/DNA BINDING PROTEIN
Compound E3 ubiquitin-protein ligase UHRF1
Source Homo sapiens (Human) (2LGG)
Sequence A:  SGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECD
MAFHIYCLDPPLSSVPSEDEWYCPECRND
B:  ARTKQTARKSTG
Description


Functional site

1) chain A
residue 315
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

2) chain A
residue 318
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

3) chain A
residue 320
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

4) chain A
residue 326
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

5) chain A
residue 328
type
sequence V
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

6) chain A
residue 329
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 380
source : AC1

7) chain A
residue 331
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 381
source : AC2

8) chain A
residue 334
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 381
source : AC2

9) chain A
residue 338
type
sequence Q
description BINDING SITE FOR RESIDUE ZN A 381
source : AC2

10) chain A
residue 354
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 381
source : AC2

11) chain A
residue 357
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 381
source : AC2

12) chain A
residue 346
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 382
source : AC3

13) chain A
residue 348
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 382
source : AC3

14) chain A
residue 349
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 382
source : AC3

15) chain A
residue 373
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 382
source : AC3

16) chain A
residue 376
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 382
source : AC3

17) chain B
residue 388
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

18) chain B
residue 384
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 385
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 386
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 343
type MOD_RES
sequence Q
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI3

22) chain B
residue 387
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 390
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

24) chain B
residue 391
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

25) chain B
residue 392
type MOD_RES
sequence S
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

26) chain B
residue 393
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI9

27) chain A
residue 315-376
type prosite
sequence CKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFH
IYCLDPPLSSVPSEDEWYCPEC
description ZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC
source prosite : PS01359


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