Research workbench
Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with AMP
Analyse Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E8O
- Type
- protein
- Length
- 1,070 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2,3-dihydroxybenzoate-AMP ligase
- UniProt
- Q47NR5
- Ligands
- AMP, SO4
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-dihydroxybenzoate-AMP ligase | protein | 536 | 35% helix, 25% strand | Q47NR5 |
| B | 2,3-dihydroxybenzoate-AMP ligase | protein | 534 | 35% helix, 25% strand | Q47NR5 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains 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 | 1043 | 0.81 | 0.82 | 118 | AMP |
| 2 | 956 | 0.80 | 0.82 | 101 | AMP |
| 3 | 804 | 0.68 | 0.75 | 70 | empty |
| 4 | 192 | 0.48 | 0.76 | 26 | empty |
| 5 | 133 | 0.44 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 278 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6E8O · Crystal structure of aryl acid adenylating enzyme FscC from Fuscachelin NRPS in complex… · 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 Q47NR5
- Elsewhere: RCSB PDB 6E8O · PDBe 6E8O · UniProt Q47NR5
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