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Influenza B/MEMPHIS/13/03 endonuclease with I38T mutation

Analyse Influenza B/MEMPHIS/13/03 endonuclease with I38T mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FSB
Type: protein
Length: 403 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein
EC: 3.1.-.-
UniProt: Q5V8Z9
Ligands: MN, MG
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase acidic protein (EC 3.1.-.-)	protein	200	50% helix, 14% strand	Q5V8Z9
B	Polymerase acidic protein (EC 3.1.-.-)	protein	203	52% helix, 15% strand	Q5V8Z9

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · chains B

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	284	0.60	0.79	33	MG
2	293	0.60	0.78	25	MN
3	72	0.33	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 131 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6FSB · Influenza B/Memphis/13/03 endonuclease with I38T mutation · 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 Q5V8Z9
Elsewhere: RCSB PDB 6FSB · PDBe 6FSB · UniProt Q5V8Z9

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