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

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Title p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9324
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 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 EYB A 402
source : AC2
6) chain A
residue 147
type
sequence V
description binding site for residue EYB A 402
source : AC2
7) chain A
residue 150
type
sequence T
description binding site for residue EYB A 402
source : AC2
8) chain A
residue 151
type
sequence P
description binding site for residue EYB A 402
source : AC2
9) chain A
residue 220
type
sequence C
description binding site for residue EYB A 402
source : AC2
10) chain A
residue 221
type
sequence E
description binding site for residue EYB A 402
source : AC2
11) chain A
residue 222
type
sequence P
description binding site for residue EYB A 402
source : AC2
12) chain A
residue 223
type
sequence P
description binding site for residue EYB A 402
source : AC2
13) chain A
residue 228
type
sequence D
description binding site for residue EYB A 402
source : AC2
14) chain A
residue 230
type
sequence T
description binding site for residue EYB A 402
source : AC2
15) chain B
residue 176
type
sequence C
description binding site for residue ZN B 401
source : AC3
16) chain B
residue 179
type
sequence H
description binding site for residue ZN B 401
source : AC3
17) chain B
residue 238
type
sequence C
description binding site for residue ZN B 401
source : AC3
18) chain B
residue 242
type
sequence C
description binding site for residue ZN B 401
source : AC3
19) chain B
residue 145
type
sequence L
description binding site for residue EYB B 402
source : AC4
20) chain B
residue 147
type
sequence V
description binding site for residue EYB B 402
source : AC4
21) chain B
residue 150
type
sequence T
description binding site for residue EYB B 402
source : AC4
22) chain B
residue 151
type
sequence P
description binding site for residue EYB B 402
source : AC4
23) chain B
residue 220
type
sequence C
description binding site for residue EYB B 402
source : AC4
24) chain B
residue 221
type
sequence E
description binding site for residue EYB B 402
source : AC4
25) chain B
residue 222
type
sequence P
description binding site for residue EYB B 402
source : AC4
26) chain B
residue 223
type
sequence P
description binding site for residue EYB B 402
source : AC4
27) chain B
residue 228
type
sequence D
description binding site for residue EYB B 402
source : AC4
28) chain B
residue 230
type
sequence T
description binding site for residue EYB B 402
source : AC4
29) chain B
residue 174
type
sequence R
description binding site for residue GOL B 403
source : AC5
30) chain B
residue 192
type
sequence Q
description binding site for residue GOL B 403
source : AC5
31) chain B
residue 207
type
sequence D
description binding site for residue GOL B 403
source : AC5
32) chain B
residue 212
type
sequence F
description binding site for residue GOL B 403
source : AC5
33) chain B
residue 214
type
sequence H
description binding site for residue GOL B 403
source : AC5
34) 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
35) 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
36) chain A
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
37) chain B
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
38) chain A
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
39) chain A
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
40) chain B
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
41) chain B
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
42) chain A
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
43) chain B
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
44) 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
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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

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