Research workbench
Crystal structure of E. faecalis DNA binding domain LIARD191N complexed with 26BP DNA
Analyse Crystal structure of E. faecalis DNA binding domain LIARD191N complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WUL
- Type
- protein + DNA
- Length
- 181 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Response regulator receiver domain protein; DNA (26-mer)
- UniProt
- R3G073
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 4 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Response regulator receiver domain protein | protein | 65 | 66% helix, 0% strand | R3G073 |
| B | Response regulator receiver domain protein | protein | 64 | 67% helix, 0% strand | R3G073 |
| H | DNA (26-mer) | dna | 26 | — | — |
| C | DNA (26-mer) | dna | 26 | — | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.56 | 0.80 | 28 | empty |
| 2 | 95 | 0.45 | 0.80 | 28 | empty |
| 3 | 72 | 0.44 | 0.82 | 25 | empty |
Interfaces
6 interfaces between chains.
- H–C · 1152 Ų buried · 119 hydrogen bonds · nucleic-nucleic
- A–B · 466 Ų buried · 5 hydrogen bonds · protein-protein
- B–H · 442 Ų buried · 13 hydrogen bonds · protein-nucleic
- A–C · 441 Ų buried · 13 hydrogen bonds · protein-nucleic
- A–H · 341 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
- 4WUL · Crystal structure of E. faecalis DNA binding domain LiaRD191N complexed with 26bp 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 R3G073
- Elsewhere: RCSB PDB 4WUL · PDBe 4WUL · UniProt R3G073
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