Research workbench

BEST1 calcium-free closed state

Analyse BEST1 calcium-free closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N26
Type: protein
Length: 1,595 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.0
Source: Gallus gallus
Molecule: Bestrophin homolog
UniProt: E1C3A0
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · resolution 3.0 · 1 distinct chain · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Bestrophin homolog	protein	319	66% helix, 0% strand	E1C3A0

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	805	0.79	0.82	62	empty
2	87	0.75	0.97	15	empty
3	75	0.75	0.98	16	empty
4	83	0.75	0.97	16	empty
5	64	0.74	0.98	15	empty

Interfaces

10 interfaces between chains.

B–C · 3993 Å² buried · 23 hydrogen bonds · protein-protein
D–E · 3965 Å² buried · 20 hydrogen bonds · protein-protein
A–E · 3934 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 3911 Å² buried · 20 hydrogen bonds · protein-protein
C–D · 3848 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

6N26 · BEST1 calcium-free closed state · 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 E1C3A0
Elsewhere: RCSB PDB 6N26 · PDBe 6N26 · UniProt E1C3A0

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