eF-site/Summary 1gzh-C

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