Research workbench

N-terminal actin-binding domain of human dystrophin

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

PDB: 1DXX
Type: protein
Length: 952 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dystrophin
UniProt: P11532
Pockets: 9 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Dystrophin	protein	238	60% helix, 1% strand	P11532

Pockets

9 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	93	0.42	0.78	30	empty
2	79	0.36	0.76	15	empty
3	58	0.34	0.78	12	empty
4	91	0.34	0.74	18	empty
5	73	0.31	0.74	17	empty

Interfaces

4 interfaces between chains.

A–B · 2572 Å² buried · 46 hydrogen bonds · protein-protein
C–D · 2569 Å² buried · 47 hydrogen bonds · protein-protein
A–D · 488 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 479 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1DXX · N-terminal Actin-binding Domain of Human Dystrophin · 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 P11532
Elsewhere: RCSB PDB 1DXX · PDBe 1DXX · UniProt P11532

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