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TRIM21

Analyse TRIM21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OLM
Type: protein
Length: 257 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase TRIM21
EC: 2.3.2.27
UniProt: P19474
Ligands: ZN
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27)	protein	125	34% helix, 20% strand	P19474
B	E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27)	protein	132	30% helix, 23% strand	P19474

Ligands and binding sites

ZN · Zinc ion · metal · 8 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.51	0.84	24	empty

Interfaces

1 interface between chains.

A–B · 1722 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

5OLM · TRIM21 · the same entry in another collection · chain A against A, TM-score 1.00
P19474 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM21 (P19474) · a predicted model of the same protein · chain B against A, TM-score 0.84

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 P19474
Elsewhere: RCSB PDB 5OLM · PDBe 5OLM · UniProt P19474

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