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Crystal structure of norwalk virus polymerase (MGSO4 crystal form)

Analyse Crystal structure of norwalk virus polymerase (MGSO4 crystal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SH3
Type: protein
Length: 1,005 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA polymerase
EC: 2.7.7.48
UniProt: Q70ET3
Ligands: MG
Pockets: 9 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA polymerase (EC 2.7.7.48)	protein	502	41% helix, 16% strand	Q70ET3
B	RNA polymerase (EC 2.7.7.48)	protein	503	41% helix, 16% strand	Q70ET3

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	747	0.72	0.78	60	empty
2	1077	0.71	0.75	76	MG
3	440	0.66	0.78	42	empty
4	379	0.63	0.78	45	empty
5	296	0.56	0.76	30	empty

Interfaces

1 interface between chains.

A–B · 389 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1SH3 · Crystal Structure of Norwalk Virus Polymerase (MgSO4 crystal form) · the same entry in another collection · chain B against B, 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 Q70ET3
Elsewhere: RCSB PDB 1SH3 · PDBe 1SH3 · UniProt Q70ET3

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