Research workbench
Designed helical protein fusion mbp
Analyse Designed helical protein fusion mbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y4C
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose binding protein fused with designed helical protein
- UniProt
- P02928
- Ligands
- GLC
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose binding protein fused with designed helical protein | protein | 480 | 55% helix, 16% strand | P02928 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.72 | 0.82 | 53 | GLC |
| 2 | 274 | 0.61 | 0.80 | 48 | empty |
| 3 | 66 | 0.39 | 0.79 | 15 | empty |
| 4 | 54 | 0.30 | 0.76 | 16 | empty |
| 5 | 57 | 0.29 | 0.74 | 13 | empty |
Compared structures
- 1Y4C · Designed Helical Protein fusion MBP · 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 P02928
- Elsewhere: RCSB PDB 1Y4C · PDBe 1Y4C · UniProt P02928
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