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Crystal structure of omsk hemorrhagic fever virus NS5 mtase (in complex with sin)

Analyse Crystal structure of omsk hemorrhagic fever virus NS5 mtase (in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V1C
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Core protein
EC: 3.4.21.91, 3.6.1.15, 3.6.4.13
UniProt: C4TPE0
Ligands: SFG
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Core protein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13)	protein	260	39% helix, 18% strand	C4TPE0

Ligands and binding sites

SFG · Sinefungin · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	596	0.67	0.77	55	GOL, SFG
2	74	0.31	0.74	17	empty

Compared structures

7V1C · Crystal structure of Omsk hemorrhagic fever virus NS5 MTase (in complex with SIN) · 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 C4TPE0
Elsewhere: RCSB PDB 7V1C · PDBe 7V1C · UniProt C4TPE0

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