Research workbench
Structure of MNTR mutant E11K complexed with Mn2+
Analyse Structure of MNTR mutant E11K complexed with Mn2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HX4
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.65
- Source
- BACILLUS SUBTILIS
- Molecule
- Transcriptional regulator mntr
- UniProt
- P54512
- Ligands
- MN
Structure
x-ray diffraction · resolution 1.65 · 1 distinct chain · 79% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcriptional regulator mntr | protein | 128 | 79% helix, 2% strand | P54512 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1298 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4HX4 · Structure of mntr mutant E11K complexed with MN2+ · the same entry in another collection · chain A against A, TM-score 1.00
- P54512 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mntr (P54512) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P54512
- Elsewhere: RCSB PDB 4HX4 · PDBe 4HX4 · UniProt P54512
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