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Crystal structure of phnf C-terminal domain
Analyse Crystal structure of phnf C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FA1
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable transcriptional regulator phnf
- UniProt
- P16684
- Ligands
- BDF
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable transcriptional regulator phnf | protein | 159 | 18% helix, 45% strand | P16684 |
Ligands and binding sites
- BDF · beta-D-fructopyranose · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.68 | 0.91 | 28 | empty |
| 2 | 94 | 0.37 | 0.75 | 21 | empty |
| 3 | 84 | 0.35 | 0.75 | 18 | empty |
| 4 | 62 | 0.32 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1750 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
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 P16684
- Elsewhere: RCSB PDB 2FA1 · PDBe 2FA1 · UniProt P16684
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