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Crystal structure of active HIV-1 protease in complex with the N terminal product of ca-P2 cleavage site
Analyse Crystal structure of active HIV-1 protease in complex with the N terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F73
- Type
- protein
- Length
- 205 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease; N terminal product of substrate ca-P2
- EC
- 3.4.23.16
- UniProt
- P03369
Structure
x-ray diffraction · 3 distinct chains · 4% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease (EC 3.4.23.16) | protein | 99 | 4% helix, 55% strand | P03369 |
| C | N terminal product of substrate ca-P2 | protein | 4 | 0% helix, 50% strand | — |
| D | N terminal product of substrate ca-P2 | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–B · 1839 Ų buried · 39 hydrogen bonds · protein-protein
- A–C · 316 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 315 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 202 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 192 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4F73 · Crystal Structure of active HIV-1 Protease in Complex with the N terminal product of… · 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
- Elsewhere: RCSB PDB 4F73 · PDBe 4F73 · UniProt P03369
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