Research workbench
14-3-3 sigma in complex with hdmx-367 peptide
Analyse 14-3-3 sigma in complex with hdmx-367 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YR5
- Type
- protein
- Length
- 943 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P31947, O15151
- Ligands
- SO4
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 229 | — | P31947 |
| O | — | protein | 9 | — | O15151 |
| B | — | protein | 228 | — | P31947 |
| P | — | protein | 10 | — | O15151 |
| C | — | protein | 225 | — | P31947 |
| Q | — | protein | 7 | — | O15151 |
| D | — | protein | 229 | — | P31947 |
| R | — | protein | 6 | — | O15151 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
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 P31947
- Every structure of UniProt O15151
- Elsewhere: RCSB PDB 6YR5 · PDBe 6YR5 · UniProt P31947 · UniProt O15151
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