MolNFT v1 · #122106 · protein
Crystal structure of polymerase acid protein (pa) from influenza a virus, wilson-SMITH/1933 (H1N1) bound to follow on fragment ebsi-4720 1-(4-bromophenyl)-1H-imidazole
5IFC · Polymerase acidic protein: “Crystal structure of polymerase acid protein (pa) from influenza a virus, wilson-SMITH/1933 (H1N1) bound to…”. X-ray diffraction, 1 ligand (6AR), 7 pockets (best druggability 0.62). MolNFT v1 #122106 on…
- PDB
- 5IFC
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polymerase acidic protein
- UniProt
- P15659
- Ligands
- 6AR
- Pockets
- 7 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polymerase acidic protein | protein | 410 | 44% helix, 19% strand | P15659 |
Ligands and binding sites
- 6AR · 1-(4-bromophenyl)-1H-imidazole · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.62 | 0.82 | 29 | DMS |
| 2 | 123 | 0.47 | 0.78 | 24 | empty |
| 3 | 54 | 0.40 | 0.81 | 14 | 6AR |
| 4 | 119 | 0.39 | 0.75 | 25 | empty |
| 5 | 65 | 0.35 | 0.77 | 19 | empty |
Compared structures
- 5IFC · Crystal structure of polymerase acid protein (PA) from Influenza A virus… · 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 P15659
- Elsewhere: RCSB PDB 5IFC · PDBe 5IFC · UniProt P15659
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