4AV1

Crystal structure of the human PARP-1 DNA binding domain in complex with DNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0008270	molecular_function	zinc ion binding
B	0003677	molecular_function	DNA binding
B	0008270	molecular_function	zinc ion binding
C	0003677	molecular_function	DNA binding
C	0008270	molecular_function	zinc ion binding
D	0003677	molecular_function	DNA binding
D	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1600

Chain	Residue
A	CYS21
A	CYS24
A	HIS53
A	CYS56

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1600

Chain	Residue
B	CYS125
B	CYS128
B	HIS159
B	CYS162

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1600

Chain	Residue
C	CYS24
C	HIS53
C	CYS56
C	CYS21

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1600

Chain	Residue
D	CYS125
D	CYS128
D	HIS159
D	CYS162

---

Functional Information from PROSITE/UniProt

site_id	PS00347
Number of Residues	36
Details	ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC

Chain	Residue	Details
A	CYS21-CYS56
A	CYS125-CYS162

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	336
Details	ZN_FING: PARP-type 1 => ECO:0000255|PROSITE-ProRule:PRU00264

Chain	Residue	Details
A	TYR9-GLY93
B	TYR9-GLY93
C	TYR9-GLY93
D	TYR9-GLY93

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB

Chain	Residue	Details
B	CYS21
B	CYS24
B	HIS53
B	CYS56
C	CYS21
C	CYS24
C	HIS53
C	CYS56
D	CYS21
D	CYS24
D	HIS53
D	CYS56
A	CYS21
A	CYS56
A	CYS24
A	HIS53

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1

Chain	Residue	Details
D	CYS125
D	CYS128
D	HIS159
D	CYS162
A	CYS125
A	CYS128
A	HIS159
A	CYS162
B	CYS125
B	CYS128
B	HIS159
B	CYS162
C	CYS125
C	CYS128
C	HIS159
C	CYS162

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	SER41
D	SER41
A	SER41
C	SER41

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
B	LYS105
B	LYS131
C	LYS97
C	LYS105
C	LYS131
D	LYS97
D	LYS105
D	LYS131
A	LYS97
A	LYS105
A	LYS131
B	LYS97

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER185
B	SER185
C	SER185
D	SER185
A	SER177
B	SER177
C	SER177
D	SER177

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER179
B	SER179
C	SER179
D	SER179

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS192
B	LYS192
C	LYS192
D	LYS192

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