Research workbench
Crystal structure of B. halodurans mntr in apo form
Analyse Crystal structure of B. halodurans mntr in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KTB
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator mntr
- UniProt
- Q9K943
- Ligands
- MN, MG, PO4
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hth-type transcriptional regulator mntr | protein | 138 | 74% helix, 6% strand | Q9K943 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains B
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · 3 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 · 1342 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6KTB · Crystal structure of B. halodurans MntR in apo form · the same entry in another collection · chain A against A, TM-score 1.00
- Q9K943 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mntr (Q9K943) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q9K943
- Elsewhere: RCSB PDB 6KTB · PDBe 6KTB · UniProt Q9K943
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