MolNFT v1 · #138495 · protein

Co-crystal structure of influenza a H3N2 PB2 (241-741) bound to vx-787

5WL0 · Polymerase basic protein 2: “Co-crystal structure of influenza a H3N2 PB2 (241-741) bound to vx-787”. X-ray diffraction, 1 ligand (21G), 3 pockets (best druggability 0.75). MolNFT v1 #138495 on GenesisL1: 3D structure, binding sites…

PDB: 5WL0
Type: protein
Length: 482 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase basic protein 2
UniProt: Q67296
Ligands: 21G
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase basic protein 2	protein	482	34% helix, 27% strand	Q67296

Ligands and binding sites

21G · (2S,3S)-3-[[5-fluoranyl-2-(5-fluoranyl-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-4-yl]amino]bicyclo[2.2.2]octane-2-carboxylic acid · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	779	0.75	0.80	96	21G
2	200	0.54	0.78	29	empty
3	63	0.27	0.73	17	empty

Compared structures

5WL0 · Co-crystal structure of Influenza A H3N2 PB2 (241-741) bound to VX-787 · 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 Q67296
Elsewhere: RCSB PDB 5WL0 · PDBe 5WL0 · UniProt Q67296

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