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Regioselective structural and functional mimicry of peptides. design of hydrolytically stable cyclic peptidomimetic inhibitors of HIV-1 protease
Analyse Regioselective structural and functional mimicry of peptides. design of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CPI
- Type
- protein
- Length
- 203 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 protease; Cyclic peptide inhibitor
- UniProt
- P03369
- Ligands
- SO4, NH2
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIV-1 protease | protein | 99 | 4% helix, 54% strand | P03369 |
| C | Cyclic peptide inhibitor | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1858 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 454 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 426 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (nonstandard).
Compared structures
- 1CPI · Regioselective structural and functional mimicry of peptides. design of hydrolytically… · 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
- Every structure of UniProt P03369
- Elsewhere: RCSB PDB 1CPI · PDBe 1CPI · UniProt P03369
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