Research workbench
Switching the chirality of the metal environment alters the coordination mode in designed peptides.
Analyse Switching the chirality of the metal environment alters the coordination mode… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H5F
- Type
- protein
- Length
- 87 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coil ser L16L-pen
- Ligands
- ACE, ZN, NH2, CL
Structure
x-ray diffraction · 1 distinct chain · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Coil ser L16L-pen | protein | 29 | 90% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 4 copies · chains A, C
- NH2 · Amino group · ion · 3 copies · chains A, B, C
- CL · Chloride ion · ion · 3 copies · chains A, B, C
- ACT · Acetate ion · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 613 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 612 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 542 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 covalent, 3 modified (covalent ligand, nonstandard).
Compared structures
- 3H5F · Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 3H5F · PDBe 3H5F
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.