MolNFT v1 · #29758 · protein

GCN4-leucine zipper core mutant ASN16ABA in the trimeric state

1ZIJ · General control protein GCN4: “GCN4-leucine zipper core mutant ASN16ABA in the trimeric state”. X-ray diffraction, 1 ligand (ACE). MolNFT v1 #29758 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	General control protein GCN4	protein	33	82% helix, 0% strand	P03069

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 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 761 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 676 Å² 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

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 1ZIJ · PDBe 1ZIJ · UniProt P03069

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