MolNFT v1 · #67595 · protein
SIVMAC239 nef in complex with a TCR zeta polypeptide DP1 (L51-D93)
3IOZ · Protein nef: “SIVMAC239 nef in complex with a TCR zeta polypeptide DP1 (L51-D93)”. X-ray diffraction, 1 pocket (best druggability 0.34). MolNFT v1 #67595 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3IOZ
- Type
- protein
- Length
- 125 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein nef; T-cell surface glycoprotein CD3 zeta chain
- UniProt
- Q5QGG3, P20963
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein nef | protein | 109 | 33% helix, 15% strand | Q5QGG3 |
| B | T-cell surface glycoprotein CD3 zeta chain | protein | 16 | 50% helix, 0% strand | P20963 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.34 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 540 Ų buried · 7 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 Q5QGG3
- Every structure of UniProt P20963
- Elsewhere: RCSB PDB 3IOZ · PDBe 3IOZ · UniProt Q5QGG3 · UniProt P20963
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