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Crystal structure of the large C-terminal domain of polymerase basic protein 2 from influenza virus A/MEXICO/INDRE4487/2009(H1N1)

Analyse Crystal structure of the large C-terminal domain of polymerase basic protein 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KHW
Type: protein
Length: 402 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase PB2
UniProt: C3W6M3
Pockets: 7 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Polymerase PB2	protein	201	36% helix, 22% strand	C3W6M3

Ligands and binding sites

GOL · Glycerol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	415	0.65	0.78	36	empty
2	139	0.43	0.76	31	empty
3	97	0.39	0.76	24	empty
4	68	0.37	0.78	18	empty
5	56	0.34	0.78	18	empty

Interfaces

1 interface between chains.

A–B · 955 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3KHW · Crystal structure of the large c-terminal domain of polymerase basic protein 2 from… · 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 C3W6M3
Elsewhere: RCSB PDB 3KHW · PDBe 3KHW · UniProt C3W6M3

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