Research workbench
Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein GP34, P21 native crystal
Analyse Crystal structure of the carboxy-terminal region of the bacteriophage T4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UXF
- Type
- protein
- Length
- 1,190 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Large tail fiber protein P34
- UniProt
- P18771
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Large tail fiber protein P34 | protein | 397 | 4% helix, 49% strand | P18771 |
| C | Large tail fiber protein P34 | protein | 396 | 3% helix, 49% strand | P18771 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.81 | 0.97 | 27 | empty |
| 2 | 66 | 0.76 | 0.98 | 23 | empty |
| 3 | 136 | 0.44 | 0.76 | 25 | GOL |
| 4 | 93 | 0.43 | 0.79 | 24 | empty |
| 5 | 101 | 0.40 | 0.76 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–C · 9089 Ų buried · 188 hydrogen bonds · protein-protein
- A–B · 9070 Ų buried · 175 hydrogen bonds · protein-protein
- B–C · 8990 Ų buried · 185 hydrogen bonds · protein-protein
Compared structures
- 4UXF · Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long… · 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 P18771
- Elsewhere: RCSB PDB 4UXF · PDBe 4UXF · UniProt P18771
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