MolNFT v1 · #156418 · protein
Crystal structure of HPF1/PARP1 complex
6M3I · Histone parylation factor 1: “Crystal structure of HPF1/PARP1 complex”. X-ray diffraction, 1 ligand (UNU), 4 pockets (best druggability 0.75). MolNFT v1 #156418 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6M3I
- Type
- protein
- Length
- 550 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone parylation factor 1; Poly [ADP-ribose] polymerase 1
- EC
- 2.4.2.30, 2.4.2.-
- UniProt
- Q9NWY4, P09874
- Ligands
- UNU
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone parylation factor 1 | protein | 316 | 48% helix, 8% strand | Q9NWY4 |
| B | Poly [ADP-ribose] polymerase 1 (EC 2.4.2.30, 2.4.2.-) | protein | 234 | 26% helix, 36% strand | P09874 |
Ligands and binding sites
- UNU · Benzamide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.75 | 0.94 | 30 | empty |
| 2 | 145 | 0.43 | 0.75 | 29 | empty |
| 3 | 85 | 0.33 | 0.73 | 18 | empty |
| 4 | 54 | 0.27 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1156 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 Q9NWY4
- Every structure of UniProt P09874
- Elsewhere: RCSB PDB 6M3I · PDBe 6M3I · UniProt Q9NWY4 · UniProt P09874
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