Research workbench
Structural and functional studies of fatty acyl-adenylate ligases from E. COLI and L. pneumophila
Analyse Structural and functional studies of fatty acyl-adenylate ligases from E. COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PBK
- Type
- protein
- Length
- 1,105 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acyl-adenylate ligase
- UniProt
- Q8FDN4
- Ligands
- 1ZZ
- Pockets
- 7 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acyl-adenylate ligase | protein | 555 | 36% helix, 24% strand | Q8FDN4 |
| B | Fatty acyl-adenylate ligase | protein | 550 | 37% helix, 23% strand | Q8FDN4 |
Ligands and binding sites
- 1ZZ · 5'-O-[(S)-(dodecanoyloxy)(hydroxy)phosphoryl]adenosine · ligand · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.87 | 0.88 | 130 | 1ZZ |
| 2 | 1132 | 0.85 | 0.86 | 134 | 1ZZ |
| 3 | 399 | 0.64 | 0.78 | 42 | empty |
| 4 | 301 | 0.58 | 0.77 | 35 | empty |
| 5 | 75 | 0.37 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 204 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 17 modified (engineered).
Compared structures
- 3PBK · Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L.… · the same entry in another collection · chain B against B, 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 Q8FDN4
- Elsewhere: RCSB PDB 3PBK · PDBe 3PBK · UniProt Q8FDN4
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