Research workbench
Crystal structure of the MN(2+)-bound form of response regulator RCP1
Analyse Crystal structure of the MN(2+)-bound form of response regulator RCP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JLK
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Response regulator RCP1
- UniProt
- Q55169
- Ligands
- MN, SO4
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Response regulator RCP1 | protein | 141 | 41% helix, 18% strand | Q55169 |
| B | Response regulator RCP1 | protein | 139 | 42% helix, 18% strand | Q55169 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1256 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1JLK · Crystal structure of the Mn(2+)-bound form of response regulator Rcp1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q55169 · AlphaFold monomer V2.0 prediction for response regulator RCP1 (Q55169) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q55169
- Elsewhere: RCSB PDB 1JLK · PDBe 1JLK · UniProt Q55169
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