Research workbench
Crystal structure analysis of the N-terminal receiver domain of response regulator pmra
Analyse Crystal structure analysis of the N-terminal receiver domain of response… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W9S
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ompr family response regulator in two-component regulatory system with bass
- UniProt
- C4X5T7
- Ligands
- BEF, MG
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ompr family response regulator in two-component regulatory system with bass | protein | 116 | 47% helix, 18% strand | C4X5T7 |
| B | Ompr family response regulator in two-component regulatory system with bass | protein | 117 | 48% helix, 18% strand | C4X5T7 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.47 | 0.77 | 22 | empty |
| 2 | 78 | 0.40 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 873 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3W9S · Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA · 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 C4X5T7
- Elsewhere: RCSB PDB 3W9S · PDBe 3W9S · UniProt C4X5T7
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