Research workbench

Fmdv 3D polymerase crystallized in presence of (F)URIDYLYLATED vpg peptide

Analyse Fmdv 3D polymerase crystallized in presence of (F)URIDYLYLATED vpg peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6S2L
Type: protein
Length: 476 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
EC: 3.4.22.46, 3.6.1.15, 3.4.22.28, 2.7.7.48
UniProt: P03311
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Genome polyprotein (EC 3.4.22.46, 3.6.1.15, 3.4.22.28, 2.7.7.48)	protein	476	42% helix, 19% strand	P03311

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

2 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	469	0.72	0.82	43	GOL
2	757	0.68	0.75	55	empty

Compared structures

6S2L · FMDV 3D polymerase crystallized in presence of (F)uridylylated VPg peptide · 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 6S2L · PDBe 6S2L · UniProt P03311

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.