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Substrate shape determines specificity of recognition recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes
Analyse Substrate shape determines specificity of recognition recognition for HIV-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KJG
- Type
- protein
- Length
- 207 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pol polyprotein; Gag polyprotein
- EC
- 3.4.23.16
- UniProt
- P03369
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pol polyprotein (EC 3.4.23.16) | protein | 99 | 4% helix, 57% strand | P03369 |
| P | Gag polyprotein | protein | 9 | 0% helix, 44% strand | — |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1840 Ų buried · 33 hydrogen bonds · protein-protein
- B–P · 530 Ų buried · 8 hydrogen bonds · protein-protein
- A–P · 522 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1KJG · Substrate shape determines specificity of recognition recognition for HIV-1 protease… · 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 1KJG · PDBe 1KJG · UniProt P03369
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