4OPX

Structure of Human PARP-1 bound to a DNA double strand break in complex with (2R)-5-fluoro-2-methyl-2,3-dihydro-1-benzofuran-7-carboxamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0008270	molecular_function	zinc ion binding
C	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
D	0003677	molecular_function	DNA binding
D	0008270	molecular_function	zinc ion binding
F	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	CYS21
A	CYS24
A	HIS53
A	CYS56

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	CYS295
A	CYS298
A	CYS311
A	CYS321

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2UR C 1101

Chain	Residue
C	GLY863
C	TYR896
C	PHE897
C	ALA898
C	LYS903
C	SER904
C	TYR907
C	HIS862

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 401

Chain	Residue
D	CYS21
D	CYS24
D	HIS53
D	CYS56

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 402

Chain	Residue
D	CYS295
D	CYS298
D	CYS311
D	CYS321

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851

Chain	Residue	Details
C	GLU988
F	GLU988

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5

Chain	Residue	Details
C	HIS862
C	GLY871
C	ARG878
C	SER904
F	HIS862
F	GLY871
F	ARG878
F	SER904

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:34210965, ECO:0000269|PubMed:34625544

Chain	Residue	Details
C	SER519
F	SER519
A	CYS311
A	CYS321
D	CYS295
D	CYS298
D	CYS311
D	CYS321

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000255

Chain	Residue	Details
C	GLU520
F	GLU520

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-(ADP-ribosyl)lysine => ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:27568560

Chain	Residue	Details
C	LYS521
F	LYS521

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:35460603

Chain	Residue	Details
C	THR594
F	THR594

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
C	LYS600
C	LYS621
F	LYS600
F	LYS621

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	SER782
F	SER782
D	SER274
D	SER277

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	SER786
F	SER786

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
C	LYS528
F	LYS528
D	LYS249

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733

Chain	Residue	Details
C	LYS748
F	LYS748

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