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Crystal structure of polymerase acid protein (pa) from influenza a virus, wilson-SMITH/1933 (H1N1) bound to follow on fragment ebsi-4721 1-(4-fluorophenyl)-1H-imidazole

Analyse Crystal structure of polymerase acid protein (pa) from influenza a virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IFD
Type: protein
Length: 408 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein
UniProt: P15659
Ligands: 6AQ
Pockets: 6 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase acidic protein	protein	408	44% helix, 19% strand	P15659

Ligands and binding sites

6AQ · 1-(4-fluorophenyl)-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

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	220	0.63	0.82	31	DMS
2	120	0.48	0.79	24	empty
3	151	0.43	0.75	30	empty
4	59	0.36	0.78	9	6AQ
5	71	0.35	0.76	14	empty

Compared structures

5IFD · 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 5IFD · PDBe 5IFD · UniProt P15659

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