Research workbench
14-3-3SIGMA in complex with SHN3PS542 phosphopeptide crystal structure
Analyse 14-3-3SIGMA in complex with SHN3PS542 phosphopeptide crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B13
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; SHN3PS542
- UniProt
- P31947
- Ligands
- MG
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 236 | 79% helix, 0% strand | P31947 |
| P | SHN3PS542 | protein | 10 | 0% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–P · 759 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, phosphorylation).
Compared structures
- 7B13 · 14-3-3sigma in complex with SHN3pS542 phosphopeptide crystal structure · the same entry in another collection · chain A against A, TM-score 1.00
- P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.95
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
- Elsewhere: RCSB PDB 7B13 · PDBe 7B13 · UniProt P31947
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