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Mutant K18E of 3D polymerase from foot-and-moth disease virus

Analyse Mutant K18E of 3D polymerase from foot-and-moth disease virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WYL
Type: protein
Length: 478 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase 3D-pol
EC: 2.7.7.48
UniProt: P03311
Ligands: MN
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-directed RNA polymerase 3D-pol (EC 2.7.7.48)	protein	478	41% helix, 19% strand	P03311

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A
GOL · Glycerol · additive · 3 copies · chains A
ACT · Acetate ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	708	0.70	0.77	64	ACT
2	190	0.42	0.72	23	empty
3	56	0.24	0.72	15	MN

Compared structures

4WYL · Mutant K18E of 3D polymerase from Foot-and-Moth Disease 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 P03311
Elsewhere: RCSB PDB 4WYL · PDBe 4WYL · UniProt P03311

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