MolNFT v1 · #113796 · protein
Darpin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography
5AQ7 · D12_DB04V3: “Darpin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein…”. X-ray diffraction, 4 pockets (best druggability 0.73). MolNFT v1 #113796 on GenesisL1: 3D structure, binding…
- PDB
- 5AQ7
- Type
- protein
- Length
- 812 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D12_DB04V3
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | D12_DB04V3 | protein | 406 | 48% helix, 11% strand | — |
Ligands and binding sites
- MLI · Malonate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1182 | 0.73 | 0.76 | 98 | empty |
| 2 | 92 | 0.38 | 0.76 | 20 | empty |
| 3 | 129 | 0.37 | 0.73 | 19 | empty |
| 4 | 51 | 0.26 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 297 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5AQ7 · 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 5AQ7 · PDBe 5AQ7
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