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CryoEM Structure of Allosterically Switchable De Novo Protein sr312, in Open State with Effector Peptide

Analyse CryoEM Structure of Allosterically Switchable De Novo Protein sr312, in Open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8URE
Type: protein
Length: 1,792 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.4
Source: synthetic construct; SYNTHETIC CONSTRUCT
Molecule: sr312; Effector peptide cs221B
Pockets: 20 · best druggability 0.80

Structure

electron microscopy · resolution 4.4 · 2 distinct chains · 73% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	sr312	protein	422	72% helix, 11% strand	—
B, D, F, H	Effector peptide cs221B	protein	26	88% helix, 0% strand	—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	876	0.80	0.83	105	empty
2	863	0.80	0.83	106	empty
3	812	0.77	0.81	107	empty
4	1169	0.77	0.79	135	empty
5	558	0.73	0.81	96	empty

Interfaces

9 interfaces between chains.

C–D · 371 Å² buried · 0 hydrogen bonds · protein-protein
G–H · 341 Å² buried · 0 hydrogen bonds · protein-protein
E–F · 332 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 316 Å² buried · 0 hydrogen bonds · protein-protein
A–G · 273 Å² buried · 7 hydrogen bonds · protein-protein

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 8URE · PDBe 8URE

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