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Crystal structure of ASK1-D3 ubiquitin ligase FORM1

Analyse Crystal structure of ASK1-D3 ubiquitin ligase FORM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BRO
Type
protein
Length
1,458 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
F-BOX/LRR-repeat MAX2 homolog; SKP1-like protein 1A
UniProt
Q5VMP0, Q39255
Pockets
19 · best druggability 0.49

Structure

x-ray diffraction · 4 distinct chains · 34% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BF-BOX/LRR-repeat MAX2 homologprotein61430% helix, 18% strandQ5VMP0
ASKP1-like protein 1Aprotein11756% helix, 3% strandQ39255
DF-BOX/LRR-repeat MAX2 homologprotein61030% helix, 18% strandQ5VMP0
CSKP1-like protein 1Aprotein11755% helix, 3% strandQ39255

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11900.490.7629empty
22290.490.7537empty
32080.480.7535empty
41840.470.7523empty
5500.460.8415empty

Interfaces

3 interfaces between chains.

  • B–A · 2086 Ų buried · 28 hydrogen bonds · protein-protein
  • D–C · 2066 Ų buried · 28 hydrogen bonds · protein-protein
  • B–D · 488 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6BRO · Crystal structure of ASK1-D3 ubiquitin ligase form1 · the same entry in another collection · chain C against C, TM-score 1.00
  • Q5VMP0 · AlphaFold monomer V2.0 prediction for F-BOX/LRR-repeat MAX2 homolog (Q5VMP0) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • Q39255 · AlphaFold monomer V2.0 prediction for SKP1-like protein 1A (Q39255) · a predicted model of the same protein · chain C against A, TM-score 0.92

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