Research workbench
A role for chey glu 89 in chez-mediated dephosphorylation of the E. COLI chemotaxis response regulator chey
Analyse A role for chey glu 89 in chez-mediated dephosphorylation of the E. COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MIH
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chey
- UniProt
- P06143
- Ligands
- BEF, MN, SO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chemotaxis protein chey | protein | 128 | 44% helix, 16% strand | P06143 |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1MIH · A role for chey glu 89 in chez-mediated dephosphorylation of the E. COLI chemotaxis… · the same entry in another collection · chain A against A, TM-score 1.00
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 P06143
- Elsewhere: RCSB PDB 1MIH · PDBe 1MIH · UniProt P06143
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