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Crystal structure of the extracellular domain of PEPT1
Analyse Crystal structure of the extracellular domain of PEPT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A9D
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute carrier family 15 member 1
- UniProt
- Q9JIP7
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Solute carrier family 15 member 1 | protein | 189 | 2% helix, 50% strand | Q9JIP7 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 657 | 0.71 | 0.79 | 59 | GOL |
| 2 | 213 | 0.54 | 0.78 | 31 | empty |
| 3 | 65 | 0.45 | 0.82 | 13 | empty |
| 4 | 54 | 0.40 | 0.82 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1751 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q9JIP7
- Elsewhere: RCSB PDB 5A9D · PDBe 5A9D · UniProt Q9JIP7
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