Research workbench
Cryo-EM structure of the basal state of the ARTEMIS:DNA-pkcs complex (see compnd 13/14)
Analyse Cryo-EM structure of the basal state of the ARTEMIS:DNA-pkcs complex (see… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TYR
- Type
- protein
- Length
- 3,957 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-dependent protein kinase catalytic subunit; Protein artemis
- EC
- 2.7.11.1, 3.1.-.-
- UniProt
- P78527, Q96SD1
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-dependent protein kinase catalytic subunit (EC 2.7.11.1) | protein | 3905 | 62% helix, 2% strand | P78527 |
| C | Protein artemis (EC 3.1.-.-) | protein | 52 | 0% helix, 0% strand | Q96SD1 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1013 | 0.87 | 0.88 | 102 | empty |
| 2 | 969 | 0.87 | 0.88 | 117 | empty |
| 3 | 529 | 0.81 | 0.87 | 79 | empty |
| 4 | 1075 | 0.81 | 0.82 | 105 | empty |
| 5 | 398 | 0.78 | 0.86 | 46 | empty |
Interfaces
1 interface between chains.
- A–C · 1850 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7TYR · Cryo-EM structure of the basal state of the Artemis:DNA-PKcs complex (see COMPND 13/14) · the same entry in another collection · chain C against C, TM-score 1.00
- Q96SD1 · AlphaFold monomer V2.0 prediction for protein artemis (Q96SD1) · a predicted model of the same protein · chain C against A, TM-score 0.30
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 P78527
- Every structure of UniProt Q96SD1
- Elsewhere: RCSB PDB 7TYR · PDBe 7TYR · UniProt P78527 · UniProt Q96SD1
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