Research workbench
Crystal structure of the C-terminal domain of GP131 from bacteriophage phikz
Analyse Crystal structure of the C-terminal domain of GP131 from bacteriophage phikz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GBF
- Type
- protein
- Length
- 739 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PHIKZ131
- UniProt
- Q8SD31
- Ligands
- MG, CL
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PHIKZ131 | protein | 369 | 14% helix, 43% strand | Q8SD31 |
| B | PHIKZ131 | protein | 370 | 16% helix, 42% strand | Q8SD31 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 460 | 0.79 | 0.87 | 58 | MG |
| 2 | 559 | 0.78 | 0.85 | 53 | empty |
| 3 | 276 | 0.65 | 0.81 | 38 | empty |
| 4 | 245 | 0.61 | 0.81 | 34 | empty |
| 5 | 130 | 0.50 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 693 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4GBF · Crystal structure of the C-terminal domain of gp131 from bacteriophage phiKZ · 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 Q8SD31
- Elsewhere: RCSB PDB 4GBF · PDBe 4GBF · UniProt Q8SD31
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