Research workbench
Cftr associated ligand (cal) PDZ bound to HPV16 E6 oncoprotein C- terminal peptide (trretql)
Analyse Cftr associated ligand (cal) PDZ bound to HPV16 E6 oncoprotein C- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JOP
- Type
- protein
- Length
- 188 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Golgi-associated PDZ and coiled-coil motif-containing protein; Protein E6
- UniProt
- Q9HD26, P03126
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Golgi-associated PDZ and coiled-coil motif-containing protein | protein | 87 | 20% helix, 44% strand | Q9HD26 |
| C, D | Protein E6 | protein | 7 | 0% helix, 43% strand | P03126 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.39 | 0.81 | 19 | empty |
| 2 | 105 | 0.36 | 0.74 | 21 | empty |
Interfaces
4 interfaces between chains.
- B–D · 533 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 429 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 381 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 175 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4JOP · CFTR Associated Ligand (CAL) PDZ bound to HPV16 E6 oncoprotein C-terminal peptide… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HD26 · AlphaFold monomer V2.0 prediction for golgi-associated PDZ and coiled-coil… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9HD26
- Every structure of UniProt P03126
- Elsewhere: RCSB PDB 4JOP · PDBe 4JOP · UniProt Q9HD26 · UniProt P03126
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