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M. xanthus encapsulin shell protein enca with T=3 symmetry

Analyse M. xanthus encapsulin shell protein enca with T=3 symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7S20
Type: protein
Length: 825 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enca
UniProt: Q1D6H4
Pockets: 11 · best druggability 0.69

Structure

electron microscopy · 2 distinct chains · 29% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Enca	protein	277	30% helix, 18% strand	Q1D6H4
C	Enca	protein	271	29% helix, 18% strand	Q1D6H4

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.69	0.97	16	empty
2	64	0.68	0.95	23	empty
3	72	0.50	0.85	17	empty
4	142	0.43	0.75	22	empty
5	170	0.42	0.73	27	empty

Interfaces

3 interfaces between chains.

A–C · 594 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 244 Å² buried · 4 hydrogen bonds · protein-protein
C–B · 244 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7S20 · M. xanthus encapsulin shell protein EncA with T=3 symmetry · 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 Q1D6H4
Elsewhere: RCSB PDB 7S20 · PDBe 7S20 · UniProt Q1D6H4

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