Research workbench
Human myelin P2 protein, K45S mutant
Analyse Human myelin P2 protein, K45S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A1H
- Type
- protein
- Length
- 399 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myelin P2 protein
- UniProt
- P02689
- Ligands
- PLM, CL
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Myelin P2 protein | protein | 133 | 14% helix, 58% strand | P02689 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 3 copies · chains A, B, C
- CL · Chloride ion · ion · 3 copies · chains A, B, C
- GOL · Glycerol · additive · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.84 | 0.94 | 35 | PLM |
| 2 | 271 | 0.83 | 0.94 | 34 | PLM |
| 3 | 353 | 0.82 | 0.91 | 35 | PLM |
| 4 | 191 | 0.53 | 0.78 | 28 | empty |
Interfaces
2 interfaces between chains.
- A–B · 521 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 283 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P02689
- Elsewhere: RCSB PDB 4A1H · PDBe 4A1H · UniProt P02689
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