Research workbench
Unveiling the mechanism behind the in-meso crystallization of membrane proteins
Analyse Unveiling the mechanism behind the in-meso crystallization of membrane proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G26
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intimin
- UniProt
- B0LBN7
- Ligands
- 97N, 97M
- Pockets
- 2 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Intimin | protein | 241 | 5% helix, 60% strand | B0LBN7 |
Ligands and binding sites
- 97N · (2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate · ligand · 3 copies · chains A
- 97M · (2R)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate · ligand · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 470 | 0.85 | 0.92 | 53 | empty |
| 2 | 56 | 0.68 | 0.96 | 18 | empty |
Compared structures
- 5G26 · Unveiling the Mechanism Behind the in-meso Crystallization of Membrane Proteins · 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 B0LBN7
- Elsewhere: RCSB PDB 5G26 · PDBe 5G26 · UniProt B0LBN7
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