Research workbench
Tetrameric ring structure of 201PHI2-1P060 from pseudomonas phage 201PHI2-1
Analyse Tetrameric ring structure of 201PHI2-1P060 from pseudomonas phage 201PHI2-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M1X
- Type
- protein
- Length
- 289 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein 201PHI2-1P060
- UniProt
- B3FK35
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein 201PHI2-1P060 | protein | 73 | 19% helix, 49% strand | B3FK35 |
| C | Uncharacterized protein 201PHI2-1P060 | protein | 71 | 20% helix, 51% strand | B3FK35 |
| D | Uncharacterized protein 201PHI2-1P060 | protein | 72 | 19% helix, 47% strand | B3FK35 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.57 | 0.78 | 28 | empty |
Interfaces
4 interfaces between chains.
- B–C · 690 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 670 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 243 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 38 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4M1X · Tetrameric ring structure of 201phi2-1p060 from Pseudomonas phage 201phi2-1 · the same entry in another collection · chain A against A, 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 B3FK35
- Elsewhere: RCSB PDB 4M1X · PDBe 4M1X · UniProt B3FK35
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