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NMR study of C-jun homodimer

Analyse NMR study of C-jun homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JUN
Type: protein
Length: 86 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-jun homodimer
UniProt: P05412
Ligands: ACE

Structure

solution nmr · 1 distinct chain · 86% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	C-jun homodimer	protein	43	86% helix, 0% strand	P05412

Ligands and binding sites

ACE · Acetyl group · ligand · 2 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 · 940 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

1JUN · NMR study of C-jun homodimer · the same entry in another collection · chain A against A, TM-score 1.00
P05412 · AlphaFold monomer V2.0 prediction for transcription factor ap-1 (P05412) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P05412
Elsewhere: RCSB PDB 1JUN · PDBe 1JUN · UniProt P05412

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