eF-site ID 4hje-ABCDEF
PDB Code 4hje
Chain A, B, C, D, E, F

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Title Crystal structure of p53 core domain in complex with DNA
Classification Transcription/DNA
Compound Cellular tumor antigen p53
Source Homo sapiens (Human) (4HJE)
Sequence A:  PLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALN
KMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNT
FRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPI
LTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRK
B:  PLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALN
KMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNT
FRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPI
LTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRK
C:  PLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALN
KMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNT
FRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPI
LTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRK
D:  PLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALN
KMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNT
FRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPI
LTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRK
E:  TCACAAGTTAGAGACAAGCCT
F:  AGGCTTGTCTCTAACTTGTGA
Description


Functional site
1) chain A
residue 176
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1
2) chain A
residue 179
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1
3) chain A
residue 238
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1
4) chain A
residue 242
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 301
source : AC1
5) chain B
residue 176
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 301
source : AC2
6) chain B
residue 179
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 301
source : AC2
7) chain B
residue 238
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 301
source : AC2
8) chain B
residue 242
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 301
source : AC2
9) chain C
residue 176
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 301
source : AC3
10) chain C
residue 179
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 301
source : AC3
11) chain C
residue 238
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 301
source : AC3
12) chain C
residue 242
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 301
source : AC3
13) chain D
residue 176
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 301
source : AC4
14) chain D
residue 179
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 301
source : AC4
15) chain D
residue 238
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 301
source : AC4
16) chain D
residue 242
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 301
source : AC4
17) 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_FI1
18) chain C
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_FI1
19) chain C
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_FI1
20) chain C
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_FI1
21) chain D
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_FI1
22) chain D
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_FI1
23) chain D
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_FI1
24) chain D
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_FI1
25) 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_FI1
26) 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_FI1
27) 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_FI1
28) 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_FI1
29) 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_FI1
30) 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_FI1
31) 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_FI1
32) chain C
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_FI1
33) chain A
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI3
34) chain B
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI3
35) chain C
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI3
36) chain D
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI3
37) 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_FI2
38) 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_FI2
39) chain C
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_FI2
40) chain D
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_FI2
41) chain A
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
42) chain A
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
43) chain B
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
44) chain B
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
45) chain C
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
46) chain C
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
47) chain D
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
48) chain D
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI4
49) chain A
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
50) chain B
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
51) chain C
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
52) chain D
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
53) 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_FI6
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_FI6
55) chain C
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_FI6
56) chain D
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_FI6
57) chain A
residue 237-249
type prosite
sequence MCNSSCMGGMNRR
description P53 p53 family signature. MCNSSCMGGMNRR
source prosite : PS00348

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