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Cryoem structure of the apo-srpi encapasulin complex from synechococcus elongatus pcc 7942

Analyse Cryoem structure of the apo-srpi encapasulin complex from synechococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6X8T
Type: protein
Length: 280 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein srpi
UniProt: Q55032
Pockets: 1 · best druggability 0.31

Structure

electron microscopy · 1 distinct chain · 23% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein srpi	protein	280	23% helix, 31% strand	Q55032

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	60	0.31	0.75	14	empty

Compared structures

6X8T · CryoEM structure of the apo-SrpI encapasulin complex from Synechococcus elongatus PCC 7942 · the same entry in another collection · chain A against A, TM-score 1.00
Q55032 · AlphaFold monomer V2.0 prediction for protein srpi (Q55032) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q55032
Elsewhere: RCSB PDB 6X8T · PDBe 6X8T · UniProt Q55032

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