Research workbench
E. COLI TRP holorepressor, orthorhombic crystal form
Analyse E. COLI TRP holorepressor, orthorhombic crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OZ9
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRP operon repressor
- UniProt
- P0A881
- Ligands
- TRP, NA, SO4
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | TRP operon repressor | protein | 104 | 79% helix, 0% strand | P0A881 |
Ligands and binding sites
- TRP · Tryptophan · ligand · chains R
- NA · Sodium ion · metal · chains R
- SO4 · Sulfate ion · ion · chains R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P0A881
- Elsewhere: RCSB PDB 2OZ9 · PDBe 2OZ9 · UniProt P0A881
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