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Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase activity of the LNX1 ring domain

Analyse Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H7R
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase lnx
EC: 6.3.2.-
UniProt: Q8TBB1
Ligands: ZN
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	E3 ubiquitin-protein ligase lnx (EC 6.3.2.-)	protein	124	31% helix, 16% strand	Q8TBB1

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.26	0.73	14	empty

Compared structures

5H7R · Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase activity of… · the same entry in another collection · chain D against D, TM-score 1.00
Q8TBB1 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase lnx (Q8TBB1) · a predicted model of the same protein · chain D against A, TM-score 0.98

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 Q8TBB1
Elsewhere: RCSB PDB 5H7R · PDBe 5H7R · UniProt Q8TBB1

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