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Cereblon isoform 4 from magnetospirillum gryphiswaldense in multiple conformations, hexagonal crystal form

Analyse Cereblon isoform 4 from magnetospirillum gryphiswaldense in multiple… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5AMK
Type
protein
Length
422 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cereblon isoform 4
UniProt
A4TVL0
Ligands
EF2, ZN
Pockets
5 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCereblon isoform 4protein1056% helix, 50% strandA4TVL0
DCereblon isoform 4protein1076% helix, 45% strandA4TVL0

Ligands and binding sites

  • EF2 · S-Thalidomide · ligand · 2 copies · chains A, B, D
  • ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
  • DMS · Dimethyl sulfoxide · additive · chains C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12020.560.7939EF2
2890.450.8021empty
3840.410.7920EF2
4870.350.7519empty
5530.320.7713empty

Interfaces

5 interfaces between chains.

  • A–D · 721 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 688 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 550 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 341 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 149 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5AMK · Cereblon isoform 4 from Magnetospirillum gryphiswaldense in multiple conformations… · the same entry in another collection · chain B against B, TM-score 1.00

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