eF-site ID 6gga-AB
PDB Code 6gga
Chain A, B

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Title p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9284
Classification DNA BINDING PROTEIN
Compound Cellular tumor antigen p53
Source (P53_HUMAN)
Sequence A:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFC
QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR
CPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHS
VVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTII
TLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRK
B:  SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKL
FCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFR
HSVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILT
IITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRK
Description


Functional site

1) chain A
residue 145
type
sequence L
description binding site for residue EY2 A 401
source : AC1

2) chain A
residue 147
type
sequence V
description binding site for residue EY2 A 401
source : AC1

3) chain A
residue 150
type
sequence T
description binding site for residue EY2 A 401
source : AC1

4) chain A
residue 220
type
sequence C
description binding site for residue EY2 A 401
source : AC1

5) chain A
residue 221
type
sequence E
description binding site for residue EY2 A 401
source : AC1

6) chain A
residue 222
type
sequence P
description binding site for residue EY2 A 401
source : AC1

7) chain A
residue 223
type
sequence P
description binding site for residue EY2 A 401
source : AC1

8) chain A
residue 228
type
sequence D
description binding site for residue EY2 A 401
source : AC1

9) chain A
residue 230
type
sequence T
description binding site for residue EY2 A 401
source : AC1

10) chain A
residue 176
type
sequence C
description binding site for residue ZN A 402
source : AC2

11) chain A
residue 179
type
sequence H
description binding site for residue ZN A 402
source : AC2

12) chain A
residue 238
type
sequence C
description binding site for residue ZN A 402
source : AC2

13) chain A
residue 242
type
sequence C
description binding site for residue ZN A 402
source : AC2

14) chain B
residue 145
type
sequence L
description binding site for residue EY2 B 401
source : AC3

15) chain B
residue 147
type
sequence V
description binding site for residue EY2 B 401
source : AC3

16) chain B
residue 150
type
sequence T
description binding site for residue EY2 B 401
source : AC3

17) chain B
residue 220
type
sequence C
description binding site for residue EY2 B 401
source : AC3

18) chain B
residue 221
type
sequence E
description binding site for residue EY2 B 401
source : AC3

19) chain B
residue 222
type
sequence P
description binding site for residue EY2 B 401
source : AC3

20) chain B
residue 223
type
sequence P
description binding site for residue EY2 B 401
source : AC3

21) chain B
residue 228
type
sequence D
description binding site for residue EY2 B 401
source : AC3

22) chain B
residue 230
type
sequence T
description binding site for residue EY2 B 401
source : AC3

23) chain B
residue 176
type
sequence C
description binding site for residue ZN B 402
source : AC4

24) chain B
residue 179
type
sequence H
description binding site for residue ZN B 402
source : AC4

25) chain B
residue 238
type
sequence C
description binding site for residue ZN B 402
source : AC4

26) chain B
residue 242
type
sequence C
description binding site for residue ZN B 402
source : AC4

27) chain A
residue 176
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 179
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 238
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 242
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 176
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 179
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 238
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 242
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 120
type SITE
sequence K
description Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 120
type SITE
sequence K
description Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 120
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4

38) chain B
residue 120
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4

39) chain A
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5

40) chain A
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5

41) chain B
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5

42) chain B
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5

43) chain A
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6

44) chain B
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6

45) chain A
residue 291
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131
source Swiss-Prot : SWS_FT_FI8

46) chain B
residue 291
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131
source Swiss-Prot : SWS_FT_FI8


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