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Crystal structure of [I11G]cycloviolacin O2
Analyse Crystal structure of [I11G]cycloviolacin O2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RMS
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.1
- Molecule
- [I11L]cycloviolacin O2; D-[I11L]cycloviolacin O2
- UniProt
- P58434
- Ligands
- SCN
Structure
x-ray diffraction · resolution 1.1 · 2 distinct chains · 17% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | [I11L]cycloviolacin O2 | protein | 30 | 17% helix, 37% strand | P58434 |
| B | D-[I11L]cycloviolacin O2 | protein | 30 | 17% helix, 37% strand | P58434 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 274 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 d-amino, 6 disulfide (D-amino acid, disulfide).
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 P58434
- Elsewhere: RCSB PDB 7RMS · PDBe 7RMS · UniProt P58434
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