eF-site ID 4ibs-ABCD
PDB Code 4ibs
Chain A, B, C, D

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Title Human p53 core domain with hot spot mutation R273H (form I)
Classification DNA BINDING PROTEIN
Compound Cellular tumor antigen p53
Source Homo sapiens (Human) (P53_HUMAN)
Sequence A:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFC
QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR
CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHS
VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTII
TLEDSSGNLLGRNSFEVHVCACPGRDRRTEEEN
B:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFC
QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR
CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHS
VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTII
TLEDSSGNLLGRNSFEVHVCACPGRDRRTEEENL
C:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFC
QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR
CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHS
VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTII
TLEDSSGNLLGRNSFEVHVCACPGRDRRTEEENL
D:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFC
QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR
CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHS
VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTII
TLEDSSGNLLGRNSFEVHVCACPGRDRRTEEENL
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 D
residue 102
type
sequence T
description BINDING SITE FOR RESIDUE EDO D 302
source : AC5
18) chain D
residue 131
type
sequence N
description BINDING SITE FOR RESIDUE EDO D 302
source : AC5
19) chain D
residue 268
type
sequence N
description BINDING SITE FOR RESIDUE EDO D 302
source : AC5
20) chain D
residue 269
type
sequence S
description BINDING SITE FOR RESIDUE EDO D 302
source : AC5
21) chain A
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
22) chain B
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
23) chain C
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
24) chain D
residue 120
type MOD_RES
sequence K
description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171
source Swiss-Prot : SWS_FT_FI4
25) chain A
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
26) chain A
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
27) chain B
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
28) chain B
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
29) chain C
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
30) chain C
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
31) chain D
residue 183
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
32) chain D
residue 269
type MOD_RES
sequence S
description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI5
33) chain A
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
34) chain B
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
35) chain C
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
36) chain D
residue 284
type MOD_RES
sequence T
description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
source Swiss-Prot : SWS_FT_FI6
37) chain A
residue 237-249
type prosite
sequence MCNSSCMGGMNRR
description P53 p53 family signature. MCNSSCMGGMNRR
source prosite : PS00348
38) 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
39) 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
40) 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
41) 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
42) 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
43) 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
44) 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
45) 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
46) 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_FI2
47) 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_FI2
48) 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_FI2
49) 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_FI2
50) 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_FI2
51) 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_FI2
52) 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_FI2
53) 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_FI2
54) 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
55) 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
56) 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_FI3
57) 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_FI3

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