Research workbench
Darpin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography
Analyse Darpin-based crystallization chaperones exploit molecular geometry as a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AQ8
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- OFF7_DB12V4
- Ligands
- SCN
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | OFF7_DB12V4 | protein | 416 | 48% helix, 12% strand | — |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 3 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.36 | 0.77 | 19 | empty |
| 2 | 76 | 0.30 | 0.73 | 17 | EPE |
| 3 | 64 | 0.30 | 0.73 | 16 | SCN |
Compared structures
- 5AQ8 · DARPin-based Crystallization Chaperones exploit Molecular Geometry as a Screening… · 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
- Elsewhere: RCSB PDB 5AQ8 · PDBe 5AQ8
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