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Crystal structure of the roq domain of human roquin

Analyse Crystal structure of the roq domain of human roquin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3X1O
Type: protein
Length: 299 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Roquin-1
UniProt: Q5TC82
Ligands: IOD

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Roquin-1	protein	149	62% helix, 7% strand	Q5TC82
B	Roquin-1	protein	150	62% helix, 7% strand	Q5TC82

Ligands and binding sites

IOD · Iodide ion · ion · 21 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 795 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3X1O · Crystal structure of the ROQ domain of human Roquin · the same entry in another collection · chain A against A, TM-score 1.00
Q5TC82 · AlphaFold monomer V2.0 prediction for roquin-1 (Q5TC82) · a predicted model of the same protein · chain A 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 Q5TC82
Elsewhere: RCSB PDB 3X1O · PDBe 3X1O · UniProt Q5TC82

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