Research workbench
Protein-protein interaction
Analyse Protein-protein interaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IZ9
- Type
- protein
- Length
- 335 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenomatous polyposis COLI protein; ACE-gly-gly-glu-ala-leu-ala-asp-NH2
- UniProt
- P25054
- Ligands
- ACE, NH2
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenomatous polyposis COLI protein | protein | 328 | 75% helix, 0% strand | P25054 |
| B | ACE-gly-gly-glu-ala-leu-ala-asp-NH2 | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.43 | 0.82 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 528 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5IZ9 · Protein-protein interaction · the same entry in another collection · chain A against A, TM-score 1.00
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 P25054
- Elsewhere: RCSB PDB 5IZ9 · PDBe 5IZ9 · UniProt P25054
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