MolNFT v1 · #6279 · protein
Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its nucleotide complexes in three crystal forms.
1F7P · Pol polyprotein: “Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its nucleotide complexes in…”. X-ray diffraction, 1 ligand (UDP), 5 pockets (best druggability 0.82). MolNFT v1 #6279 on GenesisL1: 3D…
- PDB
- 1F7P
- Type
- protein
- Length
- 347 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pol polyprotein
- EC
- 3.6.1.23
- UniProt
- P16088
- Ligands
- UDP
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pol polyprotein (EC 3.6.1.23) | protein | 116 | 3% helix, 49% strand | P16088 |
| C | Pol polyprotein (EC 3.6.1.23) | protein | 115 | 3% helix, 49% strand | P16088 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.82 | 0.95 | 32 | empty |
| 2 | 102 | 0.47 | 0.80 | 19 | empty |
| 3 | 119 | 0.43 | 0.77 | 22 | UDP |
| 4 | 103 | 0.37 | 0.75 | 25 | UDP |
| 5 | 66 | 0.33 | 0.76 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1452 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1410 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1285 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1F7P · Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its… · 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 P16088
- Elsewhere: RCSB PDB 1F7P · PDBe 1F7P · UniProt P16088
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