Research workbench
X-ray crystal structure of magi-1 PDZ1 bound to the C- terminal peptide of HPV18 E6
Analyse X-ray crystal structure of magi-1 PDZ1 bound to the C- terminal peptide of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I04
- Type
- protein
- Length
- 182 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-associated guanylate kinase, ww and PDZ domain-containing protein 1; Peptide E6
- UniProt
- Q6RHR9, P06463
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Membrane-associated guanylate kinase, ww and PDZ domain-containing protein 1 | protein | 85 | 16% helix, 40% strand | Q6RHR9 |
| C | Peptide E6 | protein | 5 | 0% helix, 40% strand | P06463 |
| D | Peptide E6 | protein | 7 | 0% helix, 43% strand | P06463 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- A–B · 618 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 525 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 473 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 37 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2I04 · X-ray crystal structure of MAGI-1 PDZ1 bound to the C-terminal peptide of HPV18 E6 · the same entry in another collection · chain A against A, TM-score 1.00
- Q6RHR9 · AlphaFold monomer V2.0 prediction for membrane-associated guanylate kinase, ww and PDZ… · a predicted model of the same protein · chain A 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 Q6RHR9
- Every structure of UniProt P06463
- Elsewhere: RCSB PDB 2I04 · PDBe 2I04 · UniProt Q6RHR9 · UniProt P06463
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