Research workbench
Structure of human DCLRE1C/ARTEMIS in complex with DNA - re-evaluation of 6WO0
Analyse Structure of human DCLRE1C/ARTEMIS in complex with DNA - re-evaluation of 6WO0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ABS
- Type
- protein + DNA
- Length
- 371 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein artemis; DNA (5'-D(P*GP*CP*GP*AP*TP*CP*AP*GP*CP*T)-3'); DNA (5'-D(*CP*AP*GP*C)-3')
- EC
- 3.1.-.-
- UniProt
- Q96SD1
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein artemis (EC 3.1.-.-) | protein | 359 | 28% helix, 24% strand | Q96SD1 |
| B | DNA (5'-D(P*GP*CP*GP*AP*TP*CP*AP*GP*CP*T)-3') | dna | 10 | — | — |
| E | DNA (5'-D(*CP*AP*GP*C)-3') | dna | 2 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.63 | 0.82 | 26 | empty |
| 2 | 274 | 0.56 | 0.77 | 33 | ZN |
| 3 | 168 | 0.48 | 0.77 | 21 | empty |
| 4 | 184 | 0.47 | 0.75 | 34 | empty |
| 5 | 139 | 0.38 | 0.73 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–E · 292 Ų buried · 7 hydrogen bonds · protein-nucleic
- A–B · 175 Ų buried · 0 hydrogen bonds · protein-nucleic
- B–E · 104 Ų buried · 6 hydrogen bonds · nucleic-nucleic
Compared structures
- 7ABS · Structure of human DCLRE1C/Artemis in complex with DNA - re-evaluation of 6WO0 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96SD1 · AlphaFold monomer V2.0 prediction for protein artemis (Q96SD1) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q96SD1
- Elsewhere: RCSB PDB 7ABS · PDBe 7ABS · UniProt Q96SD1
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