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Crystal structure of lipolytic protein G-D-S-L family from alicyclobacillus acidocaldarius subsp. acidocaldarius dsm 446
Analyse Crystal structure of lipolytic protein G-D-S-L family from alicyclobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RJT
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipolytic protein G-D-S-L family
- UniProt
- C8WT89
- Ligands
- SO4, CL
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lipolytic protein G-D-S-L family | protein | 214 | 51% helix, 11% strand | C8WT89 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.61 | 0.76 | 64 | EDO |
| 2 | 73 | 0.34 | 0.76 | 13 | empty |
| 3 | 54 | 0.31 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 973 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered, oxidation).
Compared structures
- 3RJT · Crystal structure of lipolytic protein G-D-S-L family from Alicyclobacillus… · 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 C8WT89
- Elsewhere: RCSB PDB 3RJT · PDBe 3RJT · UniProt C8WT89
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