Research workbench
Mbp-fusion protein of PILA1 residues 26-159
Analyse Mbp-fusion protein of PILA1 residues 26-159 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OGM
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose ABC transporter periplasmic protein, pilin protein chimera
- UniProt
- D8A942, A0A1R2EY47
- Ligands
- GLC
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose ABC transporter periplasmic protein, pilin protein chimera | protein | 500 | 41% helix, 23% strand | D8A942, A0A1R2EY47 |
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
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.71 | 0.86 | 31 | GLC |
| 2 | 246 | 0.49 | 0.74 | 38 | empty |
| 3 | 192 | 0.47 | 0.76 | 29 | empty |
| 4 | 71 | 0.34 | 0.76 | 17 | empty |
| 5 | 89 | 0.31 | 0.72 | 18 | empty |
Compared structures
- 4OGM · MBP-fusion protein of PilA1 residues 26-159 · 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 D8A942
- Every structure of UniProt A0A1R2EY47
- Elsewhere: RCSB PDB 4OGM · PDBe 4OGM · UniProt D8A942 · UniProt A0A1R2EY47
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