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Solution NMR structure of human REV1 (932-1039) in complex with ubiquitin

Analyse Solution NMR structure of human REV1 (932-1039) in complex with ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VZM
Type
protein
Length
187 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin; DNA repair protein REV1
EC
2.7.7.-
UniProt
P0CG47, Q9UBZ9

Structure

solution nmr · 2 distinct chains · 29% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein7624% helix, 34% strandP0CG47
BDNA repair protein REV1 (EC 2.7.7.-)protein11133% helix, 0% strandQ9UBZ9

Interfaces

1 interface between chains.

  • A–B · 678 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5VZM · Solution NMR structure of human Rev1 (932-1039) in complex with ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UBZ9 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (Q9UBZ9) · a predicted model of the same protein · chain B against A, TM-score 0.33

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