Research workbench
X-ray crystal structure of SAP97 PDZ3 bound to the C- terminal peptide of HPV18 E6
Analyse X-ray crystal structure of SAP97 PDZ3 bound to the C- terminal peptide of HPV18… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I0I
- Type
- protein
- Length
- 261 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disks large homolog 1; Peptide E6
- UniProt
- Q62696, P06463
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Disks large homolog 1 | protein | 81 | 17% helix, 36% strand | Q62696 |
| D, E, F | Peptide E6 | protein | 6 | 0% helix, 50% strand | P06463 |
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 | 157 | 0.43 | 0.75 | 26 | empty |
| 2 | 50 | 0.26 | 0.74 | 14 | empty |
Interfaces
6 interfaces between chains.
- C–F · 470 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 445 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 389 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 319 Ų buried · 7 hydrogen bonds · protein-protein
- A–E · 204 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2I0I · X-ray crystal structure of Sap97 PDZ3 bound to the C-terminal peptide of HPV18 E6 · the same entry in another collection · chain F against F, TM-score 1.00
- Q62696 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q62696) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q62696
- Every structure of UniProt P06463
- Elsewhere: RCSB PDB 2I0I · PDBe 2I0I · UniProt Q62696 · UniProt P06463
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