Research workbench
Self-assembly of coiled-coil tetramers in the 1.40 a structure of a leucine-zipper mutant
Analyse Self-assembly of coiled-coil tetramers in the 1.40 a structure of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NRN
- Type
- protein
- Length
- 128 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control protein GCN4
- UniProt
- P03069
- Ligands
- PO4
Structure
x-ray diffraction · 4 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General control protein GCN4 | protein | 30 | 93% helix, 0% strand | P03069 |
| B | General control protein GCN4 | protein | 33 | 91% helix, 0% strand | P03069 |
| C | General control protein GCN4 | protein | 31 | 90% helix, 0% strand | P03069 |
| D | General control protein GCN4 | protein | 34 | 91% helix, 0% strand | P03069 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains B, D, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–B · 805 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 804 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 594 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 338 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 121 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2NRN · Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant · the same entry in another collection · chain D against D, 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 D against A, TM-score 0.91
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 2NRN · PDBe 2NRN · UniProt P03069
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