Research workbench
Structure of arta and DNA complex
Analyse Structure of arta and DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GXQ
- Type
- protein + DNA
- Length
- 128 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative regulator of transfer genes arta; DNA (5'-D(*AP*CP*AP*TP*GP*AP*CP*AP*TP*G)-3')…
- UniProt
- Q2FDC9
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 4 distinct chains · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative regulator of transfer genes arta | protein | 53 | 53% helix, 13% strand | Q2FDC9 |
| B | Putative regulator of transfer genes arta | protein | 54 | 63% helix, 13% strand | Q2FDC9 |
| C | DNA (5'-D(*AP*CP*AP*TP*GP*AP*CP*AP*TP*G)-3') | dna | 10 | — | — |
| D | DNA (5'-D(*AP*CP*AP*TP*GP*TP*CP*AP*TP*GP*T)-3') | dna | 11 | — | — |
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 | 110 | 0.42 | 0.77 | 23 | empty |
| 2 | 98 | 0.34 | 0.74 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1717 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 469 Ų buried · 37 hydrogen bonds · nucleic-nucleic
- B–D · 332 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–C · 283 Ų buried · 12 hydrogen bonds · protein-nucleic
- A–D · 212 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 3GXQ · Structure of ArtA and DNA complex · 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 Q2FDC9
- Elsewhere: RCSB PDB 3GXQ · PDBe 3GXQ · UniProt Q2FDC9
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