eF-site ID 1gzh-C
PDB Code 1gzh
Chain C

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Title Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor
Classification GENE REGULATION
Compound CELLULAR TUMOR ANTIGEN P53
Source Homo sapiens (Human) (P53_HUMAN)
Sequence C:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMF
CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR
RCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRH
SVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI
ITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLR
Description


Functional site

1) chain C
residue 183
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 2972
source : AC2

2) chain C
residue 176
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1290
source : AC3

3) chain C
residue 179
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1290
source : AC3

4) chain C
residue 238
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1290
source : AC3

5) chain C
residue 242
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1290
source : AC3

6) chain C
residue 237-249
type prosite
sequence MCNSSCMGGMNRR
description P53 p53 family signature. MCNSSCMGGMNRR
source prosite : PS00348

7) 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

8) 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

9) 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

10) 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

11) 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

12) chain C
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

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

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

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


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