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Crystal structure of the mid, cap-binding, mid-link and 627 domains from avian influenza a virus polymerase PB2 subunit bound to M7GTP H32 crystal form

Analyse Crystal structure of the mid, cap-binding, mid-link and 627 domains from avian… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FMQ
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Influenza a PB2 subunit
UniProt: Q6DNN3
Ligands: MGT
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Influenza a PB2 subunit	protein	424	38% helix, 25% strand	Q6DNN3

Ligands and binding sites

MGT · 7N-methyl-8-hydroguanosine-5'-triphosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	417	0.73	0.83	43	MGT
2	249	0.58	0.79	39	empty
3	57	0.52	0.87	14	empty
4	109	0.45	0.78	21	empty

Compared structures

5FMQ · Crystal structure of the mid, cap-binding, mid-link and 627 domains from avian influenza… · 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 Q6DNN3
Elsewhere: RCSB PDB 5FMQ · PDBe 5FMQ · UniProt Q6DNN3

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