Research workbench

Crystal structure of human filamin C domains 14-15 cardiovascular disease causing mutation G1676R

Analyse Crystal structure of human filamin C domains 14-15 cardiovascular disease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P0E
Type: protein
Length: 404 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 2 of filamin-C
UniProt: Q14315
Pockets: 2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Isoform 2 of filamin-C	protein	202	4% helix, 51% strand	Q14315

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	83	0.32	0.73	20	empty
2	57	0.29	0.74	15	EDO

Interfaces

1 interface between chains.

A–B · 452 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7P0E · Crystal structure of human filamin C domains 14-15 cardiovascular disease causing… · 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 Q14315
Elsewhere: RCSB PDB 7P0E · PDBe 7P0E · UniProt Q14315

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.