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Crystal structure of the T3D reovirus SIGMA1 coiled coil tail and body

Analyse Crystal structure of the T3D reovirus SIGMA1 coiled coil tail and body in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GAP
Type: protein
Length: 645 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer capsid protein sigma-1
UniProt: P03528
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 3 distinct chains · 67% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer capsid protein sigma-1	protein	218	67% helix, 17% strand	P03528
B	Outer capsid protein sigma-1	protein	214	67% helix, 17% strand	P03528
C	Outer capsid protein sigma-1	protein	213	66% helix, 17% strand	P03528

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.29	0.73	14	empty

Interfaces

3 interfaces between chains.

A–C · 4501 Å² buried · 50 hydrogen bonds · protein-protein
A–B · 4499 Å² buried · 46 hydrogen bonds · protein-protein
B–C · 4477 Å² buried · 54 hydrogen bonds · protein-protein

Compared structures

6GAP · Crystal structure of the T3D reovirus sigma1 coiled coil tail and body · 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 P03528
Elsewhere: RCSB PDB 6GAP · PDBe 6GAP · UniProt P03528

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