Research workbench

Poliovirus polymerase - G289A/C290F loop mutant

Analyse Poliovirus polymerase - G289A/C290F loop mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NLV
Type: protein
Length: 461 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: P03300
Ligands: NA
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-directed RNA polymerase 3D-pol (EC 2.7.7.48)	protein	461	42% helix, 16% strand	P03300

Ligands and binding sites

NA · Sodium ion · metal · chains A
ACY · Acetic acid · additive · 8 copies · chains A
1PE · Pentaethylene glycol · additive · 2 copies · 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	671	0.70	0.78	77	ACY
2	246	0.56	0.78	29	empty
3	51	0.31	0.76	14	empty

Modifications

Observed in the structure: 3 modified (artifact).

Compared structures

4NLV · Poliovirus Polymerase - G289A/C290F Loop Mutant · 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 P03300
Elsewhere: RCSB PDB 4NLV · PDBe 4NLV · UniProt P03300

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