Research workbench
Human ARTD2 in complex with DNA oligonucleotides
Analyse Human ARTD2 in complex with DNA oligonucleotides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AEO
- Type
- protein + DNA
- Length
- 488 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly [ADP-ribose] polymerase 2; DNA
- EC
- 2.4.2.30, 2.4.2.-
- UniProt
- Q9UGN5
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poly [ADP-ribose] polymerase 2 (EC 2.4.2.30, 2.4.2.-) | protein | 456 | 31% helix, 27% strand | Q9UGN5 |
| B | DNA | dna | 16 | — | — |
| C | DNA | dna | 16 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 742 | 0.66 | 0.74 | 75 | SO4 |
| 2 | 372 | 0.54 | 0.74 | 30 | empty |
| 3 | 124 | 0.50 | 0.80 | 23 | empty |
| 4 | 96 | 0.42 | 0.78 | 23 | empty |
| 5 | 145 | 0.40 | 0.73 | 22 | empty |
Interfaces
3 interfaces between chains.
- B–C · 681 Ų buried · 68 hydrogen bonds · nucleic-nucleic
- A–C · 241 Ų buried · 7 hydrogen bonds · protein-nucleic
- A–B · 57 Ų buried · 1 hydrogen bond · protein-nucleic
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 Q9UGN5
- Elsewhere: RCSB PDB 7AEO · PDBe 7AEO · UniProt Q9UGN5
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