Research workbench
1.08 a structure of apo-chey reveals meta-active conformation
Analyse 1.08 a structure of apo-chey reveals meta-active conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JBE
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chey
- UniProt
- P0AE67
- Ligands
- SNN, SO4
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein chey | protein | 126 | 43% helix, 17% strand | P0AE67 |
Ligands and binding sites
- SNN · L-3-aminosuccinimide · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 covalent (additive adduct, covalent ligand).
Compared structures
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 1JBE · PDBe 1JBE · UniProt P0AE67
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