Research workbench
REP1-nxsq fatty acid transporter Y128F mutant
Analyse REP1-nxsq fatty acid transporter Y128F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PP6
- Type
- protein
- Length
- 392 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- REP1-ncxsq
- UniProt
- C4N147
- Ligands
- PAM
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | REP1-ncxsq | protein | 130 | 15% helix, 58% strand | C4N147 |
| B, C | REP1-ncxsq | protein | 131 | 15% helix, 57% strand | C4N147 |
Ligands and binding sites
- PAM · Palmitoleic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 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 | 0.84 | 0.92 | 37 | PAM |
| 2 | 376 | 0.83 | 0.92 | 35 | PAM |
| 3 | 392 | 0.81 | 0.90 | 36 | PAM |
| 4 | 198 | 0.47 | 0.75 | 26 | empty |
| 5 | 74 | 0.44 | 0.81 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–C · 283 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 206 Ų buried · 6 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 C4N147
- Elsewhere: RCSB PDB 3PP6 · PDBe 3PP6 · UniProt C4N147
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