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Crystal structure of actin-binding domain of mouse plectin

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

PDB
1SH5
Type
protein
Length
464 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Plectin 1
UniProt
Q9QXS1
Pockets
2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPlectin 1protein23258% helix, 0% strandQ9QXS1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19580.770.8083empty
2500.300.7615empty

Interfaces

1 interface between chains.

  • A–B · 428 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1SH5 · Crystal structure of actin-binding domain of mouse plectin · the same entry in another collection · chain A against A, TM-score 1.00

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