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Helix capping in the GCN4 leucine zipper

Analyse Helix capping in the GCN4 leucine zipper in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CE9
Type: protein
Length: 136 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (GCN4-pmse)
UniProt: P03069
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protein (GCN4-pmse)	protein	34	85% helix, 0% strand	P03069

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.49	0.76	26	empty

Interfaces

5 interfaces between chains.

C–D · 896 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 891 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 407 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 138 Å² buried · 1 hydrogen bond · protein-protein
A–D · 117 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1CE9 · Helix capping in the GCN4 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 0.85

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 1CE9 · PDBe 1CE9 · UniProt P03069

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