Research workbench

HCV-J4 NS5B polymerase point mutant orthorhombic crystal form

Analyse HCV-J4 NS5B polymerase point mutant orthorhombic crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XHV
Type: protein
Length: 1,126 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase
EC: 2.7.7.48
UniProt: O92972
Ligands: MG, SO4
Pockets: 12 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	RNA-directed RNA polymerase (EC 2.7.7.48)	protein	563	47% helix, 15% strand	O92972

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 18 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1144	0.82	0.83	84	SO4, MG
2	1134	0.81	0.83	80	SO4
3	815	0.69	0.75	81	SO4
4	118	0.50	0.80	20	empty
5	126	0.46	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 291 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2XHV · HCV-J4 NS5B Polymerase Point Mutant Orthorhombic Crystal Form · 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 O92972
Elsewhere: RCSB PDB 2XHV · PDBe 2XHV · UniProt O92972

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