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Solution NMR structure of tryptophan to alanine mutant of arkadia ring domain.

Analyse Solution NMR structure of tryptophan to alanine mutant of arkadia ring domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LG0
Type: protein
Length: 69 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase arkadia
EC: 6.3.2.-
UniProt: Q6ZNA4
Ligands: ZN
Pockets: 1 · best druggability 0.31

Structure

solution nmr · 1 distinct chain · 14% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase arkadia (EC 6.3.2.-)	protein	69	14% helix, 20% strand	Q6ZNA4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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	64	0.31	0.75	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5LG0 · Solution NMR structure of Tryptophan to Alanine mutant of Arkadia RING domain. · the same entry in another collection · chain A against A, TM-score 1.00
Q6ZNA4 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase arkadia (Q6ZNA4) · a predicted model of the same protein · chain A against A, TM-score 0.69

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 Q6ZNA4
Elsewhere: RCSB PDB 5LG0 · PDBe 5LG0 · UniProt Q6ZNA4

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