Research workbench
Pria helicase bound to ADP
Analyse Pria helicase bound to ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NL4
- Type
- protein
- Length
- 698 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Primosome assembly protein pria
- UniProt
- A6TGC5
- Ligands
- ADP, ZN
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Primosome assembly protein pria | protein | 698 | 31% helix, 23% strand | A6TGC5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 421 | 0.77 | 0.86 | 46 | empty |
| 2 | 379 | 0.77 | 0.87 | 47 | empty |
| 3 | 293 | 0.63 | 0.80 | 33 | empty |
| 4 | 218 | 0.62 | 0.82 | 28 | empty |
| 5 | 358 | 0.60 | 0.77 | 63 | ADP |
Compared structures
- 4NL4 · PriA Helicase Bound to ADP · the same entry in another collection · chain H against H, 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 A6TGC5
- Elsewhere: RCSB PDB 4NL4 · PDBe 4NL4 · UniProt A6TGC5
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