Research workbench
Crystal structure at 1.8 ångströms of the bacillus subtilis catabolite repression histidine containing protein (crh)
Analyse Crystal structure at 1.8 ångströms of the bacillus subtilis catabolite… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MU4
- Type
- protein
- Length
- 173 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hpr-like protein crh
- UniProt
- O06976
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hpr-like protein crh | protein | 86 | 34% helix, 30% strand | O06976 |
| B | Hpr-like protein crh | protein | 87 | 32% helix, 30% strand | O06976 |
Ligands and binding sites
- SO4 · Sulfate 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 · 2252 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 1MU4 · Crystal structure at 1.8 ångströms of the bacillus subtilis catabolite repression… · the same entry in another collection · chain A against A, TM-score 1.00
- O06976 · AlphaFold monomer V2.0 prediction for hpr-like protein crh (O06976) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 O06976
- Elsewhere: RCSB PDB 1MU4 · PDBe 1MU4 · UniProt O06976
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