MolNFT v1 · #179925 · protein

Structure of the catalytic domain of PARP1

7KK2 · Poly [ADP-ribose] polymerase 1: “Structure of the catalytic domain of PARP1”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.81). MolNFT v1 #179925 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7KK2
Type: protein
Length: 700 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Poly [ADP-ribose] polymerase 1
EC: 2.4.2.30, 2.4.2.-
UniProt: P09874
Ligands: SO4
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poly [ADP-ribose] polymerase 1 (EC 2.4.2.30, 2.4.2.-)	protein	351	40% helix, 25% strand	P09874
B	Poly [ADP-ribose] polymerase 1 (EC 2.4.2.30, 2.4.2.-)	protein	349	39% helix, 23% strand	P09874

Ligands and binding sites

SO4 · Sulfate ion · ion · 7 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	896	0.81	0.83	74	SO4
2	479	0.77	0.85	45	SO4
3	115	0.56	0.84	16	empty
4	79	0.46	0.82	15	empty
5	86	0.44	0.80	18	empty

Interfaces

1 interface between chains.

A–B · 837 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7KK2 · Structure of the catalytic domain of PARP1 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P09874
Elsewhere: RCSB PDB 7KK2 · PDBe 7KK2 · UniProt P09874

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.