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Hepatitis C virus RNA polymerase in complex with GTP and manganese

Analyse Hepatitis C virus RNA polymerase in complex with GTP and manganese in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GX5
Type: protein
Length: 530 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase
EC: 2.7.7.48
UniProt: P26663
Ligands: GTP, MN
Pockets: 10 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-directed RNA polymerase (EC 2.7.7.48)	protein	530	51% helix, 16% strand	P26663

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A
MN · Manganese (II) ion · metal · 3 copies · chains A

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

Pockets

10 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	419	0.62	0.77	43	empty
2	219	0.56	0.79	28	GTP
3	135	0.46	0.77	17	empty
4	98	0.40	0.77	18	empty
5	83	0.35	0.76	24	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

1GX5 · Hepatitis C Virus RNA Polymerase in Complex with GTP and Manganese · 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 P26663
Elsewhere: RCSB PDB 1GX5 · PDBe 1GX5 · UniProt P26663

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