Research workbench
Crystal structure of two-component response regulator, luxr family, from aurantimonas sp. SI85-9A1
Analyse Crystal structure of two-component response regulator, luxr family, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CZ5
- Type
- protein
- Length
- 565 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two-component response regulator, luxr family
- UniProt
- Q1YEP2
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Two-component response regulator, luxr family | protein | 141 | 43% helix, 20% strand | Q1YEP2 |
| B | Two-component response regulator, luxr family | protein | 140 | 47% helix, 20% strand | Q1YEP2 |
| C, D | Two-component response regulator, luxr family | protein | 142 | 46% helix, 20% strand | Q1YEP2 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.64 | 0.92 | 14 | empty |
| 2 | 78 | 0.29 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 25 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3CZ5 · Crystal structure of two-component response regulator, LuxR family, from Aurantimonas sp.… · 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 Q1YEP2
- Elsewhere: RCSB PDB 3CZ5 · PDBe 3CZ5 · UniProt Q1YEP2
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