Research workbench
Crystal structure of mbp-TOM20 fusion protein with a 4-residue spacer in the connector helix
Analyse Crystal structure of mbp-TOM20 fusion protein with a 4-residue spacer in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AZ7
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic PROTEIN,MITOCHONDRIAL import receptor subunit TOM20 homolog
- UniProt
- P0AEX9, Q62760
- Ligands
- GLC
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic PROTEIN,MITOCHONDRIAL import receptor subunit TOM20 homolog | protein | 434 | 51% helix, 18% strand | P0AEX9, Q62760 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.69 | 0.84 | 35 | GLC |
| 2 | 167 | 0.42 | 0.74 | 20 | empty |
| 3 | 58 | 0.31 | 0.75 | 13 | empty |
Compared structures
- 5AZ7 · Crystal structure of MBP-Tom20 fusion protein with a 4-residue spacer in the connector… · the same entry in another collection · chain A against A, TM-score 1.00
- Q62760 · AlphaFold monomer V2.0 prediction for mitochondrial import receptor subunit TOM20 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.15
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 P0AEX9
- Every structure of UniProt Q62760
- Elsewhere: RCSB PDB 5AZ7 · PDBe 5AZ7 · UniProt P0AEX9 · UniProt Q62760
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