Research workbench
Crystal structure of inactive single chain wild-type HIV-1 protease in complex with the substrate P2-nc
Analyse Crystal structure of inactive single chain wild-type HIV-1 protease in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EPJ
- Type
- protein
- Length
- 206 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease, tethered dimer; Substrate P2-nc
- EC
- 3.4.23.16
- UniProt
- P03369, Q9YP46
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease, tethered dimer (EC 3.4.23.16) | protein | 198 | 4% helix, 56% strand | P03369 |
| D | Substrate P2-nc | protein | 8 | 0% helix, 50% strand | Q9YP46 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
- ACT · Acetate ion · additive · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–D · 710 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4EPJ · Crystal Structure of inactive single chain wild-type HIV-1 Protease in Complex with the… · 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
- Every structure of UniProt Q9YP46
- Elsewhere: RCSB PDB 4EPJ · PDBe 4EPJ · UniProt P03369 · UniProt Q9YP46
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