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

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Title p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9318
Classification DNA BINDING PROTEIN
Compound Cellular tumor antigen p53
Source (P53_HUMAN)
Sequence A:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLF
CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR
RCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRH
SVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTI
ITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKK
B:  SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKL
FCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFR
HSVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILT
IITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRK
Description


Functional site

1) chain A
residue 176
type
sequence C
description binding site for residue ZN A 401
source : AC1

2) chain A
residue 179
type
sequence H
description binding site for residue ZN A 401
source : AC1

3) chain A
residue 238
type
sequence C
description binding site for residue ZN A 401
source : AC1

4) chain A
residue 242
type
sequence C
description binding site for residue ZN A 401
source : AC1

5) chain A
residue 145
type
sequence L
description binding site for residue EXQ A 402
source : AC2

6) chain A
residue 147
type
sequence V
description binding site for residue EXQ A 402
source : AC2

7) chain A
residue 150
type
sequence T
description binding site for residue EXQ A 402
source : AC2

8) chain A
residue 151
type
sequence P
description binding site for residue EXQ A 402
source : AC2

9) chain A
residue 220
type
sequence C
description binding site for residue EXQ A 402
source : AC2

10) chain A
residue 221
type
sequence E
description binding site for residue EXQ A 402
source : AC2

11) chain A
residue 222
type
sequence P
description binding site for residue EXQ A 402
source : AC2

12) chain A
residue 223
type
sequence P
description binding site for residue EXQ A 402
source : AC2

13) chain A
residue 228
type
sequence D
description binding site for residue EXQ A 402
source : AC2

14) chain A
residue 230
type
sequence T
description binding site for residue EXQ A 402
source : AC2

15) chain A
residue 131
type
sequence N
description binding site for residue EDO A 403
source : AC3

16) chain A
residue 252
type
sequence L
description binding site for residue EDO A 403
source : AC3

17) chain A
residue 269
type
sequence S
description binding site for residue EDO A 403
source : AC3

18) chain B
residue 176
type
sequence C
description binding site for residue ZN B 401
source : AC4

19) chain B
residue 179
type
sequence H
description binding site for residue ZN B 401
source : AC4

20) chain B
residue 238
type
sequence C
description binding site for residue ZN B 401
source : AC4

21) chain B
residue 242
type
sequence C
description binding site for residue ZN B 401
source : AC4

22) chain B
residue 174
type
sequence R
description binding site for residue GOL B 402
source : AC5

23) chain B
residue 192
type
sequence Q
description binding site for residue GOL B 402
source : AC5

24) chain B
residue 207
type
sequence D
description binding site for residue GOL B 402
source : AC5

25) chain B
residue 212
type
sequence F
description binding site for residue GOL B 402
source : AC5

26) chain B
residue 214
type
sequence H
description binding site for residue GOL B 402
source : AC5

27) chain A
residue 97
type
sequence V
description binding site for residue EPE B 403
source : AC6

28) chain A
residue 169
type
sequence M
description binding site for residue EPE B 403
source : AC6

29) chain B
residue 138
type
sequence A
description binding site for residue EPE B 403
source : AC6

30) chain B
residue 139
type
sequence K
description binding site for residue EPE B 403
source : AC6

31) chain B
residue 140
type
sequence T
description binding site for residue EPE B 403
source : AC6

32) chain B
residue 198
type
sequence E
description binding site for residue EPE B 403
source : AC6

33) chain B
residue 235
type
sequence N
description binding site for residue EPE B 403
source : AC6

34) chain B
residue 145
type
sequence L
description binding site for residue EXQ B 404
source : AC7

35) chain B
residue 147
type
sequence V
description binding site for residue EXQ B 404
source : AC7

36) chain B
residue 151
type
sequence P
description binding site for residue EXQ B 404
source : AC7

37) chain B
residue 220
type
sequence C
description binding site for residue EXQ B 404
source : AC7

38) chain B
residue 221
type
sequence E
description binding site for residue EXQ B 404
source : AC7

39) chain B
residue 222
type
sequence P
description binding site for residue EXQ B 404
source : AC7

40) chain B
residue 223
type
sequence P
description binding site for residue EXQ B 404
source : AC7

41) chain B
residue 228
type
sequence D
description binding site for residue EXQ B 404
source : AC7

42) chain B
residue 230
type
sequence T
description binding site for residue EXQ B 404
source : AC7

43) chain A
residue 102-292
type DNA_BIND
sequence TYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTC
PVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHER
CSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPCE
PPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTIITLEDSS
GNLLGRDSFEVRVCACPGRDRRTEEENLRKK
description DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
source Swiss-Prot : SWS_FT_FI1

44) chain A
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4

45) chain B
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4

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

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

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

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

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

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

52) 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

53) chain A
residue 292
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

54) 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

55) 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

56) 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

57) 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

58) 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

59) 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

60) 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

61) 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

62) 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

63) 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

64) 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


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