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Stggyg from low-complexity domain of fus, residues 77-82

Analyse Stggyg from low-complexity domain of fus, residues 77-82 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BZP
Type: protein
Length: 12 residues
Chains: 2
Method: electron crystallography
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-binding protein fus
UniProt: P35637
Ligands: TOE

Structure

electron crystallography · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	RNA-binding protein fus	protein	6	0% helix, 0% strand	P35637

Ligands and binding sites

TOE · 2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxyl · ligand · chains B

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

Interfaces

1 interface between chains.

A–B · 116 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6BZP · STGGYG from low-complexity domain of FUS, residues 77-82 · the same entry in another collection · chain A against A, TM-score 1.00
P35637 · AlphaFold monomer V2.0 prediction for RNA-binding protein fus (P35637) · a predicted model of the same protein · chain B against A, TM-score 0.55

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 P35637
Elsewhere: RCSB PDB 6BZP · PDBe 6BZP · UniProt P35637

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