Research workbench
14-3-3 sigma with PIN1 binding site PS72 and covalently bound LVD1008
Analyse 14-3-3 sigma with PIN1 binding site PS72 and covalently bound LVD1008 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NIG
- Type
- protein
- Length
- 235 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Peptidyl-prolyl cis-trans isomerase nima-interacting 1
- EC
- 5.2.1.8
- UniProt
- P31947, Q13526
- Ligands
- UFH, CA, CL
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 228 | 82% helix, 0% strand | P31947 |
| P | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8) | protein | 7 | 0% helix, 0% strand | Q13526 |
Ligands and binding sites
- UFH · 2-bromanyl-4-imidazol-1-yl-benzaldehyde · ligand · chains A, P
- CA · Calcium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.47 | 0.81 | 20 | UFH |
| 2 | 97 | 0.36 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–P · 571 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (covalent ligand, oxidation, phosphorylation).
Compared structures
- 7NIG · 14-3-3 sigma with Pin1 binding site pS72 and covalently bound LvD1008 · 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 0.96
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 Q13526
- Elsewhere: RCSB PDB 7NIG · PDBe 7NIG · UniProt P31947 · UniProt Q13526
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