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Solution structure of the human MMS2-ubiquitin complex

Analyse Solution structure of the human MMS2-ubiquitin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZGU
Type
protein
Length
215 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-conjugating enzyme E2 variant 2; Ubiquitin
UniProt
Q15819, P61864
Pockets
2 · best druggability 0.36

Structure

solution nmr · 2 distinct chains · 25% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin-conjugating enzyme E2 variant 2protein13926% helix, 19% strandQ15819
BUbiquitinprotein7624% helix, 34% strandP61864

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.360.7915empty
2600.300.7516empty

Interfaces

1 interface between chains.

  • A–B · 657 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1ZGU · Solution structure of the human Mms2-Ubiquitin complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q15819 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2 variant 2 (Q15819) · a predicted model of the same protein · chain A against A, TM-score 0.94

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