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Structure of human REV7 in complex with a human REV3 fragment in a monoclinic crystal

Analyse Structure of human REV7 in complex with a human REV3 fragment in a monoclinic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ABD
Type
protein
Length
418 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitotic spindle assembly checkpoint protein MAD2B; DNA polymerase zeta catalytic subunit
UniProt
Q9UI95, O60673
Pockets
4 · best druggability 0.68

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitotic spindle assembly checkpoint protein MAD2Bprotein18037% helix, 34% strandQ9UI95
XDNA polymerase zeta catalytic subunitprotein2133% helix, 19% strandO60673
BMitotic spindle assembly checkpoint protein MAD2Bprotein19535% helix, 31% strandQ9UI95
YDNA polymerase zeta catalytic subunitprotein2232% helix, 18% strandO60673

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.680.9619empty
21820.470.7623empty
3530.310.7717empty
4610.300.7516empty

Interfaces

3 interfaces between chains.

  • A–X · 1152 Ų buried · 14 hydrogen bonds · protein-protein
  • B–Y · 1113 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 667 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 3ABD · Structure of human REV7 in complex with a human REV3 fragment in a monoclinic crystal · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UI95 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD2B… · a predicted model of the same protein · chain A against A, TM-score 0.99

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