Research workbench
GCN4 leucine zipper mutant with two vxxnxxx motifs coordinating chloride
Analyse GCN4 leucine zipper mutant with two vxxnxxx motifs coordinating chloride in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WPZ
- Type
- protein
- Length
- 96 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control protein GCN4
- UniProt
- P03069
- Ligands
- ACE, CL
Structure
x-ray diffraction · 3 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General control protein GCN4 | protein | 31 | 94% helix, 0% strand | P03069 |
| B | General control protein GCN4 | protein | 32 | 91% helix, 0% strand | P03069 |
| C | General control protein GCN4 | protein | 33 | 88% helix, 0% strand | P03069 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- CL · Chloride ion · ion · 2 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 · 795 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 734 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 689 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 2WPZ · GCN4 leucine zipper mutant with two VxxNxxx motifs coordinating chloride · 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 0.92
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 2WPZ · PDBe 2WPZ · UniProt P03069
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