Research workbench
The crystal structure of yeja - an ABC peptide transporter receptor
Analyse The crystal structure of yeja - an ABC peptide transporter receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ATR
- Type
- protein
- Length
- 591 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein yeja
- UniProt
- P33913
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein yeja | protein | 580 | 29% helix, 23% strand | P33913 |
| B | Uncharacterized protein yeja | protein | 11 | 36% helix, 0% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A
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 | 568 | 0.79 | 0.85 | 64 | empty |
| 2 | 494 | 0.77 | 0.84 | 58 | empty |
| 3 | 82 | 0.53 | 0.84 | 19 | GOL |
| 4 | 90 | 0.40 | 0.77 | 18 | empty |
| 5 | 74 | 0.40 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1097 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7ATR · The Crystal Structure of YejA - an ABC Peptide Transporter Receptor · the same entry in another collection · chain A against A, TM-score 1.00
- P33913 · AlphaFold monomer V2.0 prediction for uncharacterized protein yeja (P33913) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P33913
- Elsewhere: RCSB PDB 7ATR · PDBe 7ATR · UniProt P33913
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