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Crystal structure of polymerase acid protein (pa) from influenza a virus, wilson-SMITH/1933 (H1N1) bound to fragment hit ebsi-747 1-(4- chlorophenyl)-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: 5IEQ
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: 1CI
Pockets: 5 · 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	408	44% helix, 19% strand	P15659

Ligands and binding sites

1CI · 1-(4-chlorophenyl)-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

5 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	228	0.62	0.81	32	DMS
2	157	0.45	0.76	30	empty
3	133	0.39	0.74	23	empty
4	86	0.33	0.74	16	empty
5	64	0.32	0.76	13	empty

Compared structures

5IEQ · 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 5IEQ · PDBe 5IEQ · UniProt P15659

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