Research workbench
DNA-bound PRN1 helix bundle domain with ATP and magnesium in the interaction buffer
Analyse DNA-bound PRN1 helix bundle domain with ATP and magnesium in the interaction… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GVQ
- Type
- protein + DNA
- Length
- 124 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*CP*TP*GP*TP*GP*CP*TP*CP*A)-3'); Functional PRN1 primase
- UniProt
- Q54324
- Pockets
- 2 · best druggability 0.48
Structure
solution nmr · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA (5'-D(*CP*TP*GP*TP*GP*CP*TP*CP*A)-3') | dna | 9 | — | — |
| B | Functional PRN1 primase | protein | 115 | 65% helix, 0% strand | Q54324 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.48 | 0.81 | 19 | empty |
| 2 | 111 | 0.43 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 717 Ų buried · 5 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6GVQ · DNA-bound pRN1 helix bundle domain with ATP and magnesium in the interaction buffer · 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 Q54324
- Elsewhere: RCSB PDB 6GVQ · PDBe 6GVQ · UniProt Q54324
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.