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Structure of the actin-binding domain of human filamin a

Analyse Structure of the actin-binding domain of human filamin a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HOP
Type: protein
Length: 457 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Filamin-a
UniProt: P21333
Ligands: PO4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Filamin-a	protein	226	58% helix, 0% strand	P21333
B	Filamin-a	protein	231	57% helix, 0% strand	P21333

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1007	0.79	0.80	89	empty

Interfaces

1 interface between chains.

A–B · 523 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3HOP · Structure of the actin-binding domain of human filamin A · 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 0.97

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 3HOP · PDBe 3HOP · UniProt P21333

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