Research workbench
Crystal structure of a tyrosine 3-MONOOXYGENASE/TRYPTOPHAN 5- monooxygenase activation protein, beta polypeptide (ywhab) from homo sapiens at 2.20 a resolution.
Analyse Crystal structure of a tyrosine 3-MONOOXYGENASE/TRYPTOPHAN 5- monooxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DNK
- Type
- protein
- Length
- 466 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein BETA/ALPHA
- UniProt
- P31946
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein BETA/ALPHA | protein | 232 | 82% helix, 0% strand | P31946 |
| B | 14-3-3 protein BETA/ALPHA | protein | 234 | 81% helix, 0% strand | P31946 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.56 | 0.75 | 31 | EDO |
| 2 | 303 | 0.55 | 0.76 | 26 | EDO |
| 3 | 95 | 0.35 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1230 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 4DNK · Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation… · the same entry in another collection · chain A against A, TM-score 1.00
- P31946 · AlphaFold monomer V2.0 prediction for 14-3-3 protein BETA/ALPHA (P31946) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P31946
- Elsewhere: RCSB PDB 4DNK · PDBe 4DNK · UniProt P31946
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