Research workbench
Crystal structure of the star-related lipid transfer protein (fragment 25-204) from xanthomonas axonopodis at the resolution 2.4A, northeast structural genomics consortium target XAR342
Analyse Crystal structure of the star-related lipid transfer protein (fragment 25-204)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QSZ
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Star-related lipid transfer protein
- UniProt
- Q8PPZ5
- Ligands
- MN, SO4
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Star-related lipid transfer protein | protein | 177 | 20% helix, 42% strand | Q8PPZ5 |
| B | Star-related lipid transfer protein | protein | 179 | 20% helix, 42% strand | Q8PPZ5 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 489 | 0.84 | 0.90 | 46 | empty |
| 2 | 433 | 0.84 | 0.91 | 50 | empty |
| 3 | 161 | 0.41 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 419 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3QSZ · Crystal Structure of the STAR-related lipid transfer protein (fragment 25-204) from… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8PPZ5
- Elsewhere: RCSB PDB 3QSZ · PDBe 3QSZ · UniProt Q8PPZ5
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