Research workbench
Crystal structure of feline immunodeficiency virus protease complexed with a substrate
Analyse Crystal structure of feline immunodeficiency virus protease complexed with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FIV
- Type
- protein
- Length
- 234 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Feline immunodeficiency virus protease; ACE-aln-val-leu-ala-glu-aln-NH2
- EC
- 3.4.23.16
- UniProt
- P16088
- Ligands
- ACE, NH2, SO4
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Feline immunodeficiency virus protease (EC 3.4.23.16) | protein | 111 | 8% helix, 53% strand | P16088 |
| I, J | ACE-aln-val-leu-ala-glu-aln-NH2 | protein | 6 | 0% helix, 67% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, I, J, B
- NH2 · Amino group · ion · 2 copies · chains A, B, I, J
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–B · 1845 Ų buried · 38 hydrogen bonds · protein-protein
- A–J · 556 Ų buried · 8 hydrogen bonds · protein-protein
- B–I · 554 Ų buried · 8 hydrogen bonds · protein-protein
- A–I · 499 Ų buried · 4 hydrogen bonds · protein-protein
- B–J · 495 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 4 covalent (covalent ligand, nonstandard, oxidation).
Compared structures
- 3FIV · Crystal structure of feline immunodeficiency virus protease complexed with a substrate · 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 P16088
- Elsewhere: RCSB PDB 3FIV · PDBe 3FIV · UniProt P16088
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