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PanDDA analysis group deposition -- Crystal Structure of TRIM21 in complex with Z56978034

Analyse PanDDA analysis group deposition -- Crystal Structure of TRIM21 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7HMV
Type: protein
Length: 185 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.15
Source: Mus musculus
Molecule: E3 ubiquitin-protein ligase TRIM21
EC: 2.3.2.27
UniProt: Q62191
Ligands: U2R, SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · resolution 1.15 · 1 distinct chain · 5% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27)	protein	185	5% helix, 37% strand	Q62191

Ligands and binding sites

U2R · (4-fluorophenoxy)acetic acid · ligand · chains B
SO4 · Sulfate ion · ion · chains B
EDO · 1,2-ethanediol · additive

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	173	0.48	0.76	26	empty

Compared structures

Q62191 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM21 (Q62191) · 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 Q62191
Elsewhere: RCSB PDB 7HMV · PDBe 7HMV · UniProt Q62191

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