Research workbench
Structure of the chey-MN2+ complex with substitutions at 59 and 89: N59D E89Q
Analyse Structure of the chey-MN2+ complex with substitutions at 59 and 89: N59D E89Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RVK
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chey
- UniProt
- P0AE67
- Ligands
- MN
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein chey | protein | 129 | 44% helix, 17% strand | P0AE67 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3RVK · Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D E89Q · the same entry in another collection · chain A against A, TM-score 1.00
- P0AE67 · AlphaFold monomer V2.0 prediction for chemotaxis protein chey (P0AE67) · 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 P0AE67
- Elsewhere: RCSB PDB 3RVK · PDBe 3RVK · UniProt P0AE67
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