Research workbench
HIV protease (pr) dimer in closed form with pepstatin in active site and fragment 1F1-N in the OUTSIDE/TOP of flap
Analyse HIV protease (pr) dimer in closed form with pepstatin in active site and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EJK
- Type
- protein
- Length
- 203 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease; Pepstatin
- EC
- 3.4.23.16
- UniProt
- P12499
- Ligands
- IVA, IOP
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease (EC 3.4.23.16) | protein | 99 | 7% helix, 52% strand | P12499 |
| N | Pepstatin | protein | 5 | 0% helix, 40% 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 · 1855 Ų buried · 34 hydrogen bonds · protein-protein
- B–N · 466 Ų buried · 10 hydrogen bonds · protein-protein
- A–N · 442 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4EJK · HIV Protease (PR) dimer in closed form with pepstatin in active site and fragment 1F1-N… · 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 P12499
- Elsewhere: RCSB PDB 4EJK · PDBe 4EJK · UniProt P12499
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