Research workbench
GCN4PLI derivative with ALPHA/BETA/CYCLIC-gamma amino acid substitution pattern
Analyse GCN4PLI derivative with ALPHA/BETA/CYCLIC-gamma amino acid substitution pattern in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HJB
- Type
- protein
- Length
- 118 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GCN4PLI(ALPHA/BETA/CYCLIC-gamma)
- Ligands
- ACE
Structure
x-ray diffraction · 2 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | GCN4PLI(ALPHA/BETA/CYCLIC-gamma) | protein | 30 | 80% helix, 0% strand | — |
| A, B | GCN4PLI(ALPHA/BETA/CYCLIC-gamma) | protein | 29 | 93% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains C, A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- C–A · 840 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 787 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 153 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 152 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 modified, 4 covalent (nonstandard, covalent ligand).
Compared structures
- 4HJB · GCN4pLI derivative with alpha/beta/cyclic-gamma amino acid substitution pattern · the same entry in another collection · chain D against D, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4HJB · PDBe 4HJB
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