Research workbench
Crystal structure of the receiver domain of cpxr from E. COLI (tetragonal form)
Analyse Crystal structure of the receiver domain of cpxr from E. COLI (tetragonal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UHS
- Type
- protein
- Length
- 378 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein cpxr
- UniProt
- P0AE88
- Ligands
- MG
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Transcriptional regulatory protein cpxr | protein | 126 | 48% helix, 18% strand | P0AE88 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 686 | 0.71 | 0.78 | 77 | empty |
| 2 | 112 | 0.42 | 0.77 | 20 | empty |
| 3 | 62 | 0.31 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1482 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 310 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 272 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4UHS · Crystal structure of the receiver domain of CpxR from E. coli (tetragonal form) · the same entry in another collection · chain A against A, TM-score 1.00
- P0AE88 · AlphaFold monomer V2.0 prediction for transcriptional regulatory protein cpxr (P0AE88) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 P0AE88
- Elsewhere: RCSB PDB 4UHS · PDBe 4UHS · UniProt P0AE88
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