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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