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Crystal structure of the dnac helicase loader in complex with ADP-BEF3
Analyse Crystal structure of the dnac helicase loader in complex with ADP-BEF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ECC
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA replication protein dnac
- UniProt
- O67056
- Ligands
- ADP, BEF, MG
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA replication protein dnac | protein | 182 | 47% helix, 14% strand | O67056 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- BEF · Beryllium trifluoride ion · ligand · chains A
- MG · Magnesium ion · metal · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.40 | 0.75 | 23 | ADP, MG, BEF |
| 2 | 87 | 0.34 | 0.74 | 13 | empty |
| 3 | 52 | 0.31 | 0.77 | 16 | empty |
Compared structures
- 3ECC · Crystal structure of the DnaC helicase loader in complex with ADP-BeF3 · the same entry in another collection · chain A against A, TM-score 1.00
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 O67056
- Elsewhere: RCSB PDB 3ECC · PDBe 3ECC · UniProt O67056
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