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GCN4-leucine zipper core mutant ASN16ABA in the trimeric state

Analyse GCN4-leucine zipper core mutant ASN16ABA in the trimeric state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZIJ
Type
protein
Length
99 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
General control protein GCN4
UniProt
P03069
Ligands
ACE

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CGeneral control protein GCN4protein3382% helix, 0% strandP03069

Ligands and binding sites

  • ACE · Acetyl group · ligand · 3 copies · chains A, B, C

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

Interfaces

3 interfaces between chains.

  • B–C · 837 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 761 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 676 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent, 3 modified (covalent ligand, nonstandard).

Compared structures

  • 1ZIJ · GCN4-leucine zipper core mutant ASN16ABA in the trimeric state · 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 0.89

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