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Native structure of farnesyl pyrophosphate synthase from pseudomonas aeruginosa PAO1, with bound fragment KM10833.
Analyse Native structure of farnesyl pyrophosphate synthase 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
- 3ZL6
- Type
- protein
- Length
- 547 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Geranyltranstransferase
- EC
- 2.5.1.10
- UniProt
- Q9HWY4
- Ligands
- NVU, MG
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Geranyltranstransferase (EC 2.5.1.10) | protein | 273 | 75% helix, 1% strand | Q9HWY4 |
| B | Geranyltranstransferase (EC 2.5.1.10) | protein | 274 | 74% helix, 1% strand | Q9HWY4 |
Ligands and binding sites
- NVU · 2-(1,2-benzoxazol-3-yl)ethanoic acid · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 3 copies · chains A, B
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A, B
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 | 451 | 0.66 | 0.78 | 51 | DMS, MG, NVU |
| 2 | 469 | 0.64 | 0.77 | 55 | DMS, MG |
| 3 | 206 | 0.52 | 0.77 | 35 | empty |
| 4 | 180 | 0.48 | 0.76 | 30 | empty |
| 5 | 60 | 0.47 | 0.84 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1959 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3ZL6 · Native structure of Farnesyl Pyrophosphate Synthase from Pseudomonas aeruginosa PAO1… · 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 Q9HWY4
- Elsewhere: RCSB PDB 3ZL6 · PDBe 3ZL6 · UniProt Q9HWY4
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