Research workbench
Crystal structure of the extra-cellular domain of human myelin protein zero
Analyse Crystal structure of the extra-cellular domain of human myelin protein zero in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OAI
- Type
- protein
- Length
- 976 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein, myelin protein P0
- UniProt
- D3QK41, P25189
- Ligands
- GLC
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Maltose-binding periplasmic protein, myelin protein P0 | protein | 488 | 35% helix, 28% strand | D3QK41, P25189 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 362 | 0.72 | 0.83 | 33 | GLC |
| 2 | 328 | 0.71 | 0.84 | 33 | GLC |
| 3 | 531 | 0.70 | 0.80 | 57 | empty |
| 4 | 94 | 0.40 | 0.77 | 17 | empty |
| 5 | 90 | 0.38 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 385 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3OAI · Crystal structure of the extra-cellular domain of human myelin protein zero · the same entry in another collection · chain A against A, TM-score 1.00
- P25189 · AlphaFold monomer V2.0 prediction for myelin protein P0 (P25189) · a predicted model of the same protein · chain A against A, TM-score 0.24
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 D3QK41
- Every structure of UniProt P25189
- Elsewhere: RCSB PDB 3OAI · PDBe 3OAI · UniProt D3QK41 · UniProt P25189
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