Research workbench
Crystal structure of the N-terminal domain of pqsa in complex with anthraniloyl-AMP (crystal form 2)
Analyse Crystal structure of the N-terminal domain of pqsa in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OE4
- Type
- protein
- Length
- 771 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anthranilate--CoA ligase
- EC
- 6.2.1.32
- UniProt
- Q9I4X3
- Ligands
- 3UK
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anthranilate--CoA ligase (EC 6.2.1.32) | protein | 384 | 34% helix, 25% strand | Q9I4X3 |
| B | Anthranilate--CoA ligase (EC 6.2.1.32) | protein | 387 | 33% helix, 25% strand | Q9I4X3 |
Ligands and binding sites
- 3UK · 5'-O-[(S)-[(2-aminobenzoyl)oxy](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
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 857 | 0.70 | 0.76 | 72 | empty |
| 2 | 304 | 0.59 | 0.77 | 50 | 3UK |
| 3 | 159 | 0.56 | 0.82 | 31 | 3UK |
| 4 | 68 | 0.55 | 0.87 | 20 | empty |
| 5 | 69 | 0.52 | 0.86 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 105 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- Q9I4X3 · AlphaFold monomer V2.0 prediction for anthranilate--CoA ligase (Q9I4X3) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9I4X3
- Elsewhere: RCSB PDB 5OE4 · PDBe 5OE4 · UniProt Q9I4X3
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