Research workbench
Pseudomonas aeruginosa RHLG/NADP active-site complex
Analyse Pseudomonas aeruginosa RHLG/NADP active-site complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B4Q
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase
- EC
- 1.1.1.100
- UniProt
- Q9RPT1
- Ligands
- NAP
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 256 | 46% helix, 14% strand | Q9RPT1 |
| B | Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 248 | 49% helix, 14% strand | Q9RPT1 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.78 | 0.85 | 59 | NAP |
| 2 | 532 | 0.75 | 0.83 | 54 | empty |
| 3 | 168 | 0.47 | 0.76 | 20 | empty |
| 4 | 52 | 0.34 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1637 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 Q9RPT1
- Elsewhere: RCSB PDB 2B4Q · PDBe 2B4Q · UniProt Q9RPT1
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