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Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide

Analyse Structure of a dystrophin ww domain fragment in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EG4
Type: protein
Length: 273 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-dystroglycan; Dystrophin
UniProt: Q14118, P11532
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	Beta-dystroglycan	protein	13	0% helix, 0% strand	Q14118
A	Dystrophin	protein	260	59% helix, 8% strand	P11532

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	108	0.33	0.73	19	empty
2	61	0.27	0.73	13	empty

Interfaces

1 interface between chains.

P–A · 516 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1EG4 · Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide · the same entry in another collection · chain P against P, TM-score 1.00
Q14118 · AlphaFold monomer V2.0 prediction for dystroglycan (Q14118) · a predicted model of the same protein · chain P against A, TM-score 0.31

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 Q14118
Every structure of UniProt P11532
Elsewhere: RCSB PDB 1EG4 · PDBe 1EG4 · UniProt Q14118 · UniProt P11532

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