MolNFT v1 · #6758 · protein

NMR solution structure of a designed heterodimeric leucine zipper

1FMH · General control protein GCN4: “NMR solution structure of a designed heterodimeric leucine zipper”. Solution nmr, 2 ligands (ACE, NH2). MolNFT v1 #6758 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FMH
Type: protein
Length: 62 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General control protein GCN4
UniProt: P03069
Ligands: ACE, NH2

Structure

solution nmr · 2 distinct chains · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	General control protein GCN4	protein	31	90% helix, 0% strand	P03069
B	General control protein GCN4	protein	31	94% helix, 0% strand	P03069

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains A, B
NH2 · Amino group · ion · 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 · 13 hydrogen bonds · protein-protein

Modifications

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

Compared structures

1FMH · NMR solution structure of a designed heterodimeric leucine zipper · the same entry in another collection · chain A against A, TM-score 1.00
P03069 · AlphaFold monomer V2.0 prediction for general control transcription factor GCN4 (P03069) · a predicted model of the same protein · chain A 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 P03069
Elsewhere: RCSB PDB 1FMH · PDBe 1FMH · UniProt P03069

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