Research workbench
The PDZ-domain of SNTB1 complexed with the PDZ-binding motif of HPV35- E6
Analyse The PDZ-domain of SNTB1 complexed with the PDZ-binding motif of HPV35- E6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P70
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein E6; Beta-1-SYNTROPHIN,ANNEXIN A2
- UniProt
- P27228, Q13884, P07355
- Ligands
- CA
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Protein E6 | protein | 7 | 0% helix, 43% strand | P27228 |
| A | Beta-1-SYNTROPHIN,ANNEXIN A2 | protein | 407 | 60% helix, 9% strand | Q13884, P07355 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 657 | 0.68 | 0.76 | 58 | GOL |
| 2 | 156 | 0.51 | 0.79 | 35 | GOL |
| 3 | 70 | 0.32 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- C–A · 541 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7P70 · The PDZ-domain of SNTB1 complexed with the PDZ-binding motif of HPV35-E6 · the same entry in another collection · chain C against C, TM-score 1.00
- P07355 · AlphaFold monomer V2.0 prediction for annexin A2 (P07355) · a predicted model of the same protein · chain A against A, TM-score 0.79
- Q13884 · AlphaFold monomer V2.0 prediction for beta-1-syntrophin (Q13884) · a predicted model of the same protein · chain A against A, TM-score 0.27
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 P27228
- Every structure of UniProt Q13884
- Every structure of UniProt P07355
- Elsewhere: RCSB PDB 7P70 · PDBe 7P70 · UniProt P27228 · UniProt Q13884 · UniProt P07355
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