Research workbench
Crystal structure of inla S192N G194S+S/HEC1 complex
Analyse Crystal structure of inla S192N G194S+S/HEC1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OMX
- Type
- protein
- Length
- 569 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Internalin-a; Epithelial-cadherin
- UniProt
- P25146, P12830
- Ligands
- CA, CL
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Internalin-a | protein | 462 | 16% helix, 22% strand | P25146 |
| B | Epithelial-cadherin | protein | 107 | 0% helix, 45% strand | P12830 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.70 | 0.83 | 44 | empty |
| 2 | 133 | 0.50 | 0.80 | 23 | empty |
| 3 | 79 | 0.35 | 0.76 | 21 | empty |
| 4 | 60 | 0.31 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1532 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 P25146
- Every structure of UniProt P12830
- Elsewhere: RCSB PDB 2OMX · PDBe 2OMX · UniProt P25146 · UniProt P12830
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