Research workbench
Crystal structure of the phop receiver domain from bacillus subtilis
Analyse Crystal structure of the phop receiver domain from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MVO
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phop response regulator
- UniProt
- P13792
- Ligands
- NA, MN
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phop response regulator | protein | 121 | 44% helix, 20% strand | P13792 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1MVO · Crystal structure of the PhoP receiver domain from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- P13792 · AlphaFold monomer V2.0 prediction for alkaline phosphatase synthesis transcriptional… · a predicted model of the same protein · chain A 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 P13792
- Elsewhere: RCSB PDB 1MVO · PDBe 1MVO · UniProt P13792
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.