MolNFT v2 · #222378 · protein

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

8URE: “CryoEM Structure of Allosterically Switchable De Novo Protein sr312, in Open State with Effector Peptide”. Electron microscopy at 4.4, 20 pockets (best druggability 0.80). MolNFT v2 #222378 on GenesisL1: 3D structure, binding sites…

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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