Research workbench
Structure of ARTEMIS/DCLRE1C/SNM1C in complex with ceftriaxone
Analyse Structure of ARTEMIS/DCLRE1C/SNM1C in complex with ceftriaxone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7APV
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein artemis
- EC
- 3.1.-.-
- UniProt
- Q96SD1
- Ligands
- 9F2, ZN, NI
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein artemis (EC 3.1.-.-) | protein | 358 | 29% helix, 25% strand | Q96SD1 |
Ligands and binding sites
- 9F2 · Ceftriaxone · ligand · chains A
- ZN · Zinc ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.55 | 0.81 | 28 | empty |
| 2 | 170 | 0.52 | 0.79 | 30 | empty |
| 3 | 138 | 0.44 | 0.76 | 28 | EDO |
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 Q96SD1
- Elsewhere: RCSB PDB 7APV · PDBe 7APV · UniProt Q96SD1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.