Research workbench
HIV-1 nef protein in complex with engineered hck-SH3 domain
Analyse HIV-1 nef protein in complex with engineered hck-SH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3REB
- Type
- protein
- Length
- 339 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein nef; Tyrosine-protein kinase hck
- EC
- 2.7.10.2
- UniProt
- P03407, P08631
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 24% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein nef | protein | 106 | 35% helix, 13% strand | P03407 |
| B | Tyrosine-protein kinase hck (EC 2.7.10.2) | protein | 59 | 5% helix, 47% strand | P08631 |
| C | Protein nef | protein | 114 | 32% helix, 12% strand | P03407 |
| D | Tyrosine-protein kinase hck (EC 2.7.10.2) | protein | 60 | 5% helix, 47% strand | P08631 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 695 | 0.72 | 0.78 | 56 | empty |
| 2 | 68 | 0.41 | 0.80 | 16 | empty |
| 3 | 67 | 0.39 | 0.79 | 16 | empty |
| 4 | 106 | 0.36 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- C–D · 764 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 724 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 335 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P03407
- Every structure of UniProt P08631
- Elsewhere: RCSB PDB 3REB · PDBe 3REB · UniProt P03407 · UniProt P08631
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