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Complex structures of mouse RPN13 (22-130AA) and ubiquitin

Analyse Complex structures of mouse RPN13 (22-130AA) and ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z59
Type
protein
Length
185 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein ADRM1; Ubiquitin
UniProt
Q9JKV1, P62988
Pockets
1 · best druggability 0.40

Structure

solution nmr · 2 distinct chains · 16% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein ADRM1protein10915% helix, 49% strandQ9JKV1
BUbiquitinprotein7618% helix, 32% strandP62988

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.400.7718empty

Interfaces

1 interface between chains.

  • A–B · 602 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 2Z59 · Complex Structures of Mouse Rpn13 (22-130aa) and ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9JKV1 · AlphaFold monomer V2.0 prediction for proteasomal ubiquitin receptor ADRM1 (Q9JKV1) · a predicted model of the same protein · chain A against A, TM-score 0.96

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