4HHY

Crystal structure of PARP catalytic domain in complex with novel inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
B	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
C	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
D	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 15R A 401

Chain	Residue
A	LEU108
A	TYR235
A	SER243
A	TYR246
A	GLU327
A	PEG403
A	HOH508
A	HOH520
A	ASP109
A	HIS201
A	GLY202
A	ARG217
A	ILE218
A	ALA219
A	TYR228
A	GLY233

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	LYS242
A	LEU323
A	LEU324
A	TYR325

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 403

Chain	Residue
A	ASP109
A	GLY210
A	ILE211
A	GLN214
A	GLY215
A	ARG217
A	15R401
A	HOH531

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 15R B 401

Chain	Residue
B	TYR49
B	ASP109
B	HIS201
B	GLY202
B	ARG217
B	ILE218
B	ALA219
B	TYR228
B	GLY233
B	TYR235
B	SER243
B	TYR246
B	HOH510

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 402

Chain	Residue
B	LYS242
B	LEU323
B	LEU324
B	TYR325

---

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 15R C 401

Chain	Residue
C	LEU108
C	ASP109
C	VAL112
C	HIS201
C	GLY202
C	ARG217
C	ILE218
C	ALA219
C	GLY233
C	TYR235
C	PHE236
C	SER243
C	TYR246

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 15R D 401

Chain	Residue
D	LEU108
D	ASP109
D	VAL112
D	HIS201
D	GLY202
D	ARG217
D	ILE218
D	ALA219
D	PRO220
D	TYR228
D	GLY233
D	TYR235
D	PHE236
D	SER243
D	TYR246

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851

Chain	Residue	Details
A	GLU327
B	GLU327
C	GLU327
D	GLU327

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5

Chain	Residue	Details
A	HIS201
C	GLY210
C	ARG217
C	SER243
D	HIS201
D	GLY210
D	ARG217
D	SER243
A	GLY210
A	ARG217
A	SER243
B	HIS201
B	GLY210
B	ARG217
B	SER243
C	HIS201

---

site_id	SWS_FT_FI3
Number of Residues	4
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
A	SER121
B	SER121
C	SER121
D	SER121

---

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

Chain	Residue	Details
A	SER125
B	SER125
C	SER125
D	SER125

---

site_id	SWS_FT_FI5
Number of Residues	8
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
A	LYS87
B	LYS87
C	LYS87
D	LYS87

---