MolNFT v1 · #109168 · protein + DNA
Crystal structure of E. faecalis DNA binding domain LIARD191N complexed with 26BP DNA
4WUL · Response regulator receiver domain protein: “Crystal structure of E. faecalis DNA binding domain LIARD191N complexed with 26BP DNA”. X-ray diffraction, 3 pockets (best druggability 0.56). MolNFT v1 #109168 on GenesisL1: 3D…
- 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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