Research workbench

Mutant M16A of RNA dependent RNA polymerase 3D from foot-and-mouth disease virus

Analyse Mutant M16A of RNA dependent RNA polymerase 3D from foot-and-mouth disease virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GVV
Type: protein
Length: 480 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA polymerase 3D
EC: 3.4.22.46, 3.6.1.15, 3.4.22.28, 2.7.7.48
UniProt: P03311
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA polymerase 3D (EC 3.4.22.46, 3.6.1.15, 3.4.22.28, 2.7.7.48)	protein	480	40% helix, 17% strand	P03311

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

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	923	0.70	0.75	80	empty
2	109	0.42	0.77	17	empty
3	112	0.41	0.76	19	empty

Compared structures

6GVV · Mutant M16A of RNA dependent RNA polymerase 3D from Foot-and-Mouth 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 6GVV · PDBe 6GVV · UniProt P03311

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