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Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide gly-ala-gln-thr-PHE*TYR-val-asp-gly-ala
Analyse Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NXM
- Type
- protein
- Length
- 206 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease retropepsin; Analogue of rt-rh pol protease substrate peptide
- EC
- 3.4.23.16
- UniProt
- O38732
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease retropepsin (EC 3.4.23.16) | protein | 99 | 4% helix, 55% strand | O38732 |
| P | Analogue of rt-rh pol protease substrate peptide | protein | 8 | 0% helix, 50% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 1781 Ų buried · 37 hydrogen bonds · protein-protein
- B–P · 507 Ų buried · 8 hydrogen bonds · protein-protein
- A–P · 503 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2NXM · Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide… · 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 O38732
- Elsewhere: RCSB PDB 2NXM · PDBe 2NXM · UniProt O38732
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