MolNFT v1 · #66384 · protein

Structure of the actin-binding domain of human filamin a (reduced)

3HOR · Filamin-a: “Structure of the actin-binding domain of human filamin a (reduced)”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.77). MolNFT v1 #66384 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3HOR
Type: protein
Length: 420 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Filamin-a
UniProt: P21333
Ligands: PO4
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Filamin-a	protein	210	57% helix, 0% strand	P21333
B	Filamin-a	protein	210	55% helix, 0% strand	P21333

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	879	0.77	0.80	78	empty
2	71	0.36	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 609 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3HOR · Structure of the actin-binding domain of human filamin A (reduced) · the same entry in another collection · chain A against A, TM-score 1.00
P21333 · AlphaFold monomer V2.0 prediction for filamin-a (P21333) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P21333
Elsewhere: RCSB PDB 3HOR · PDBe 3HOR · UniProt P21333

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