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Elimination of the C-cap in ubiquitin structure, dynamics and thermodynamic consequences

Analyse Elimination of the C-cap in ubiquitin structure, dynamics and thermodynamic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZW7
Type
protein
Length
82 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin
UniProt
P61864
Pockets
1 · best druggability 0.72

Structure

solution nmr · 1 distinct chain · 15% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein8215% helix, 22% strandP61864

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14110.720.8345empty

Compared structures

  • 1ZW7 · Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences · the same entry in another collection · chain A against A, TM-score 1.00

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