Research workbench
HIV-1 protease in complex with the inhibitor BEA428
Analyse HIV-1 protease in complex with the inhibitor BEA428 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EC2
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 protease
- EC
- 3.4.23.16
- UniProt
- P03366
- Ligands
- BEJ
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIV-1 protease (EC 3.4.23.16) | protein | 99 | 7% helix, 55% strand | P03366 |
Ligands and binding sites
- BEJ · N,N-[2,5-O-[di-4-pyridin-3-yl-benzyl]-glucaryl]-di-[valyl-amido-methane] · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.72 | 0.83 | 41 | BEJ |
Interfaces
1 interface between chains.
- A–B · 1859 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 1EC2 · HIV-1 protease in complex with the inhibitor BEA428 · 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 P03366
- Elsewhere: RCSB PDB 1EC2 · PDBe 1EC2 · UniProt P03366
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