MolNFT v1 · #10179 · protein

Coiled coil trimer GCN4-pvls ser at buried D position

1IJ0 · General control protein GCN4: “Coiled coil trimer GCN4-pvls ser at buried D position”. X-ray diffraction, 2 ligands (ACE, ZN). MolNFT v1 #10179 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1IJ0
Type: protein
Length: 93 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General control protein GCN4
UniProt: P03069
Ligands: ACE, ZN

Structure

x-ray diffraction · 1 distinct chain · 94% helix, 0% strand (DSSP).

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

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains A, B, C
ZN · Zinc ion · metal · 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.

A–B · 757 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 723 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 664 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

1IJ0 · Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position · 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 C against A, TM-score 0.93

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 1IJ0 · PDBe 1IJ0 · UniProt P03069

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