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Crystal structure of reovirus attachment protein SIGMA1 trimer

Analyse Crystal structure of reovirus attachment protein SIGMA1 trimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KKE
Type: protein
Length: 617 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sigma 1 protein
UniProt: P03528
Pockets: 7 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Sigma 1 protein	protein	206	4% helix, 55% strand	P03528
B	Sigma 1 protein	protein	205	4% helix, 55% strand	P03528

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	473	0.87	0.95	46	empty
2	349	0.52	0.73	31	empty
3	88	0.47	0.80	16	empty
4	149	0.42	0.74	17	empty
5	67	0.39	0.79	17	empty

Interfaces

3 interfaces between chains.

B–C · 2146 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 1887 Å² buried · 27 hydrogen bonds · protein-protein
A–C · 1769 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

1KKE · Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer · 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 1KKE · PDBe 1KKE · UniProt P03528

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