Research workbench
Crystal structure of aimr in complex with DNA
Analyse Crystal structure of aimr in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JG8
- Type
- protein + DNA
- Length
- 839 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aimr transcriptional regulator; DNA (31-mer)
- UniProt
- O64094
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aimr transcriptional regulator | protein | 386 | 71% helix, 0% strand | O64094 |
| B | Aimr transcriptional regulator | protein | 393 | 70% helix, 0% strand | O64094 |
| C | DNA (31-mer) | dna | 30 | — | — |
| D | DNA (31-mer) | dna | 30 | — | — |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 883 | 0.75 | 0.78 | 84 | empty |
| 2 | 787 | 0.69 | 0.76 | 53 | empty |
| 3 | 543 | 0.69 | 0.78 | 56 | empty |
| 4 | 268 | 0.60 | 0.80 | 42 | empty |
| 5 | 237 | 0.58 | 0.80 | 39 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1483 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1322 Ų buried · 134 hydrogen bonds · nucleic-nucleic
- B–C · 434 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–D · 432 Ų buried · 10 hydrogen bonds · protein-nucleic
- A–C · 312 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
- 6JG8 · Crystal structure of AimR in complex with DNA · 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 O64094
- Elsewhere: RCSB PDB 6JG8 · PDBe 6JG8 · UniProt O64094
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