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Crystal structure of the T1L reovirus sigma1 coiled coil tail (iodide)

Analyse Crystal structure of the T1L reovirus sigma1 coiled coil tail (iodide) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GAJ
Type: protein
Length: 393 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.35
Source: Mammalian orthoreovirus 1 Lang
Molecule: Outer capsid protein sigma-1
UniProt: P04506
Ligands: CL, IOD

Structure

x-ray diffraction · resolution 1.35 · 2 distinct chains · 98% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer capsid protein sigma-1	protein	131	97% helix, 0% strand	P04506
B, C	Outer capsid protein sigma-1	protein	131	98% helix, 0% strand	P04506

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A, B, C
IOD · Iodide ion · ion · 3 copies · chains A, B, C

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

Interfaces

3 interfaces between chains.

B–C · 2651 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 2646 Å² buried · 24 hydrogen bonds · protein-protein
A–B · 2607 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

6GAJ · Crystal structure of the T1L reovirus SIGMA1 coiled coil tail (iodide) · 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 P04506
Elsewhere: RCSB PDB 6GAJ · PDBe 6GAJ · UniProt P04506

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