MolNFT v1 · #81888 · protein

Structure of FBXL5 hemerythrin domain, C2 cell

3V5X · F-BOX/LRR-repeat protein 5: “Structure of FBXL5 hemerythrin domain, C2 cell”. X-ray diffraction, 1 ligand (FEO), 2 pockets (best druggability 0.78). MolNFT v1 #81888 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3V5X
Type: protein
Length: 303 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: 2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	F-BOX/LRR-repeat protein 5	protein	151	85% helix, 0% strand	Q9UKA1
B	F-BOX/LRR-repeat protein 5	protein	152	85% helix, 0% strand	Q9UKA1

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

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1078	0.78	0.79	65	empty
2	209	0.50	0.76	22	empty

Interfaces

1 interface between chains.

A–B · 739 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3V5X · Structure of FBXL5 hemerythrin domain, C2 cell · 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 B against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9UKA1
Elsewhere: RCSB PDB 3V5X · PDBe 3V5X · UniProt Q9UKA1

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