Research workbench
Crystal structure of E.COLI ompf porin in lipidic cubic phase: space group H32, small unit cell
Analyse Crystal structure of E.COLI ompf porin in lipidic cubic phase: space group H32… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3POQ
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ompf protein
- UniProt
- C5W2U9
- Ligands
- SCN
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ompf protein | protein | 340 | 4% helix, 61% strand | C5W2U9 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 3 copies · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 23 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 937 | 0.70 | 0.75 | 67 | SCN |
| 2 | 279 | 0.49 | 0.73 | 43 | empty |
Compared structures
- 3POQ · Crystal structure of E.coli OmpF porin in lipidic cubic phase: space group H32, small… · 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 C5W2U9
- Elsewhere: RCSB PDB 3POQ · PDBe 3POQ · UniProt C5W2U9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.