Research workbench
Crystal structure analysis of HIV-1 protease mutant V82A with a substrate analog P6-pr
Analyse Crystal structure analysis of HIV-1 protease mutant V82A with a substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AOH
- Type
- protein
- Length
- 208 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pol polyprotein; Peptide inhibitor
- EC
- 3.4.23.16
- UniProt
- P04587
- Ligands
- NA, CL
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pol polyprotein (EC 3.4.23.16) | protein | 99 | 4% helix, 55% strand | P04587 |
| C | Peptide inhibitor | protein | 10 | 0% helix, 50% 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 · 1879 Ų buried · 35 hydrogen bonds · protein-protein
- B–C · 582 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 507 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 2AOH · Crystal structure analysis of HIV-1 Protease mutant V82A with a substrate analog P6-PR · 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 P04587
- Elsewhere: RCSB PDB 2AOH · PDBe 2AOH · UniProt P04587
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