MolNFT v1 · #167847 · protein

Bestrophin-2 CA2+- unbound state 1 (egta only)

6VX9: “Bestrophin-2 CA2+- unbound state 1 (egta only)”. Electron microscopy, 1 ligand (CL), 20 pockets (best druggability 0.81). MolNFT v1 #167847 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6VX9
Type: protein
Length: 1,825 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bestrophin
UniProt: E1BF86
Ligands: CL
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 65% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E, B, C, D	Bestrophin	protein	365	65% helix, 1% strand	E1BF86

Ligands and binding sites

CL · Chloride ion · ion · chains A, E, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.81	0.82	91	empty
2	888	0.78	0.80	116	CL
3	53	0.70	0.97	15	empty
4	51	0.69	0.97	15	empty
5	200	0.69	0.86	29	empty

Interfaces

10 interfaces between chains.

E–D · 5133 Å² buried · 34 hydrogen bonds · protein-protein
B–C · 5127 Å² buried · 34 hydrogen bonds · protein-protein
A–E · 5126 Å² buried · 34 hydrogen bonds · protein-protein
C–D · 5124 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 5122 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

6VX9 · bestrophin-2 Ca2+- unbound state 1 (EGTA only) · 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 E1BF86
Elsewhere: RCSB PDB 6VX9 · PDBe 6VX9 · UniProt E1BF86

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