MolNFT v1 · #90632 · protein
Crystal structure of inactive single chain wild-type HIV-1 protease in complex with the substrate rt-rh
4EP2 · Protease, tethered dimer: “Crystal structure of inactive single chain wild-type HIV-1 protease in complex with the substrate rt-rh”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #90632 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4EP2
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease, tethered dimer; Substrate rt-rh
- EC
- 3.4.23.16
- UniProt
- P03369, Q9YV20
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease, tethered dimer (EC 3.4.23.16) | protein | 198 | 4% helix, 55% strand | P03369 |
| B | Substrate rt-rh | protein | 7 | 0% helix, 43% strand | Q9YV20 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 760 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4EP2 · 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 Q9YV20
- Elsewhere: RCSB PDB 4EP2 · PDBe 4EP2 · UniProt P03369 · UniProt Q9YV20
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