Research workbench
Crystallographic studies on a family of cellular lipophilic transport proteins. refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol
Analyse Crystallographic studies on a family of cellular lipophilic transport proteins.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PMP
- Type
- protein
- Length
- 393 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P2 myelin protein
- UniProt
- P02690
- Ligands
- OLA
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | P2 myelin protein | protein | 131 | 11% helix, 56% strand | P02690 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.82 | 0.91 | 34 | OLA |
| 2 | 389 | 0.82 | 0.90 | 34 | OLA |
| 3 | 478 | 0.81 | 0.89 | 47 | OLA |
| 4 | 164 | 0.45 | 0.75 | 25 | empty |
| 5 | 54 | 0.24 | 0.73 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 572 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 153 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1PMP · Crystallographic studies on a family of cellular lipophilic transport proteins.… · the same entry in another collection · chain A against A, TM-score 1.00
- P02690 · AlphaFold monomer V2.0 prediction for myelin P2 protein (P02690) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P02690
- Elsewhere: RCSB PDB 1PMP · PDBe 1PMP · UniProt P02690
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