eF-site ID 1saf_58-ABCD
PDB Code 1saf
Model 58
Chain A, B, C, D

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Title HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)
Classification ANTI-ONCOGENE
Compound TUMOR SUPPRESSOR P53
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE
PG
B:  KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE
PG
C:  KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE
PG
D:  KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE
PG
Description


Functional site

1) chain A
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P02340
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P02340
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P02340
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P02340
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 333
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 333
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI2

7) chain C
residue 333
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI2

8) chain D
residue 333
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI2

9) chain A
residue 335
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

10) chain A
residue 337
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 335
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 337
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

13) chain C
residue 335
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

14) chain C
residue 337
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

15) chain D
residue 335
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

16) chain D
residue 337
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 351
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

18) chain D
residue 351
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

19) chain D
residue 357
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

20) chain A
residue 357
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

21) chain B
residue 351
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

22) chain B
residue 357
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

23) chain C
residue 351
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4

24) chain C
residue 357
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443
source Swiss-Prot : SWS_FT_FI4


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