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Structure of the TRIM25 coiled-coil

Analyse Structure of the TRIM25 coiled-coil in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CFG
Type: protein
Length: 326 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 UBIQUITIN/ISG15 ligase TRIM25
EC: 6.3.2.19, 6.3.2.-
UniProt: Q14258

Structure

x-ray diffraction · 2 distinct chains · 87% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 UBIQUITIN/ISG15 ligase TRIM25 (EC 6.3.2.19, 6.3.2.-)	protein	164	87% helix, 0% strand	Q14258
B	E3 UBIQUITIN/ISG15 ligase TRIM25 (EC 6.3.2.19, 6.3.2.-)	protein	162	86% helix, 0% strand	Q14258

Interfaces

1 interface between chains.

A–B · 5008 Å² buried · 31 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4CFG · Structure of the TRIM25 coiled-coil · the same entry in another collection · chain A against A, TM-score 1.00
Q14258 · AlphaFold monomer V2.0 prediction for E3 UBIQUITIN/ISG15 ligase TRIM25 (Q14258) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 Q14258
Elsewhere: RCSB PDB 4CFG · PDBe 4CFG · UniProt Q14258

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