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Structure of the ampr effector binding domain from citrobacter freundii
Analyse Structure of the ampr effector binding domain from citrobacter freundii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KOS
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional activator ampr
- UniProt
- P12529
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional activator ampr | protein | 200 | 37% helix, 29% strand | P12529 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.59 | 0.85 | 22 | MES |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 3KOS · Structure of the AmpR effector binding domain from Citrobacter freundii · the same entry in another collection · chain A against A, TM-score 1.00
- P12529 · AlphaFold monomer V2.0 prediction for hth-type transcriptional activator ampr (P12529) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P12529
- Elsewhere: RCSB PDB 3KOS · PDBe 3KOS · UniProt P12529
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