MolNFT v1 · #20317 · protein
Antiparallel trimer of GCN4-leucine zipper core mutant as N16A tetragonal form
1RB6 · General control protein GCN4: “Antiparallel trimer of GCN4-leucine zipper core mutant as N16A tetragonal form”. X-ray diffraction, 3 ligands (ACE, K, CL). MolNFT v1 #20317 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1RB6
- 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, K, 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 | 33 | 88% helix, 0% strand | P03069 |
| B | General control protein GCN4 | protein | 32 | 94% helix, 0% strand | P03069 |
| C | General control protein GCN4 | protein | 31 | 90% helix, 0% strand | P03069 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- K · Potassium ion · metal · 2 copies · chains A, B, C
- CL · Chloride ion · ion · 8 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–C · 802 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 724 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 654 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 1RB6 · Antiparallel trimer of GCN4-leucine zipper core mutant as N16A tetragonal form · 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 0.87
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 1RB6 · PDBe 1RB6 · UniProt P03069
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