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RAS1 guanine nucleotide exchange factor CDC25 (rem and catalytic domains)

Analyse RAS1 guanine nucleotide exchange factor CDC25 (rem and catalytic domains) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NZZ
Type
protein
Length
840 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cell division control protein 25
UniProt
P43069
Pockets
8 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACell division control protein 25protein42166% helix, 3% strandP43069
BCell division control protein 25protein41964% helix, 3% strandP43069

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18470.680.7590empty
21270.400.7418empty
3940.370.7520empty
41060.350.7318empty
5760.340.7514empty

Interfaces

1 interface between chains.

  • A–B · 592 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7NZZ · Ras1 guanine nucleotide exchange factor Cdc25 (REM and catalytic domains) · the same entry in another collection · chain A against A, TM-score 1.00
  • P43069 · AlphaFold monomer V2.0 prediction for cell division control protein 25 (P43069) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

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