Research workbench
Yaeo bound to magnesium from vibrio cholerae O395
Analyse Yaeo bound to magnesium from vibrio cholerae O395 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JIE
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yaeo
- UniProt
- A0A0H3ADN9
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Yaeo | protein | 77 | 13% helix, 48% strand | A0A0H3ADN9 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 517 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6JIE · YaeO bound to Magnesium from Vibrio cholerae O395 · the same entry in another collection · chain B against B, 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 A0A0H3ADN9
- Elsewhere: RCSB PDB 6JIE · PDBe 6JIE · UniProt A0A0H3ADN9
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