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Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically

Analyse Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V5Z
Type
protein
Length
309 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
F-BOX/LRR-repeat protein 5
UniProt
Q9UKA1
Ligands
FEO
Pockets
1 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AF-BOX/LRR-repeat protein 5protein15484% helix, 0% strandQ9UKA1
BF-BOX/LRR-repeat protein 5protein15583% helix, 0% strandQ9UKA1

Ligands and binding sites

  • FEO · Mu-oxo-diiron · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110200.820.8377empty

Interfaces

1 interface between chains.

  • A–B · 931 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3V5Z · Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UKA1 · AlphaFold monomer V2.0 prediction for F-BOX/LRR-repeat protein 5 (Q9UKA1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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