Research workbench
Structure of the HDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide
Analyse Structure of the HDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OQS
- Type
- protein
- Length
- 98 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disks large homolog 1; C-terminal HPV-18 E6 peptide
- UniProt
- Q12959
Structure
solution nmr · 2 distinct chains · 14% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disks large homolog 1 | protein | 92 | 15% helix, 30% strand | Q12959 |
| B | C-terminal HPV-18 E6 peptide | protein | 6 | 0% helix, 50% strand | — |
Interfaces
1 interface between chains.
- A–B · 456 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2OQS · Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q12959 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q12959) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q12959
- Elsewhere: RCSB PDB 2OQS · PDBe 2OQS · UniProt Q12959
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