Research workbench
The structure of a-pgs from pseudomonas aeruginosa
Analyse The structure of a-pgs from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V35
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanyl-tRNA-dependent L-alanyl- phophatidylglycerol synthase
- EC
- 2.3.2.11
- UniProt
- Q9I537
- Ligands
- CA, NA, SO4, CL
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alanyl-tRNA-dependent L-alanyl- phophatidylglycerol synthase (EC 2.3.2.11) | protein | 321 | 37% helix, 28% strand | Q9I537 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · 7 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.72 | 0.81 | 41 | ACT |
| 2 | 129 | 0.58 | 0.84 | 23 | GOL |
| 3 | 99 | 0.46 | 0.80 | 17 | empty |
| 4 | 92 | 0.39 | 0.76 | 15 | empty |
| 5 | 55 | 0.28 | 0.74 | 16 | empty |
Compared structures
- 4V35 · The Structure of A-PGS from Pseudomonas aeruginosa · 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 Q9I537
- Elsewhere: RCSB PDB 4V35 · PDBe 4V35 · UniProt Q9I537
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