MolNFT v1 · #106014 · protein
Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target
4RMF · Aspartate--TRNA(ASP/ASN) ligase: “Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb…”. X-ray diffraction, 1 ligand (3SY), 6 pockets (best druggability 0.73). MolNFT v1…
- PDB
- 4RMF
- Type
- protein
- Length
- 579 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate--TRNA(ASP/ASN) ligase
- EC
- 6.1.1.23
- UniProt
- A0QWN3
- Ligands
- 3SY
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate--TRNA(ASP/ASN) ligase (EC 6.1.1.23) | protein | 579 | 31% helix, 25% strand | A0QWN3 |
Ligands and binding sites
- 3SY · 2,2-bis(hydroxymethyl)propane-1,3-diol · ligand · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 714 | 0.73 | 0.79 | 59 | FMT |
| 2 | 94 | 0.40 | 0.77 | 24 | empty |
| 3 | 136 | 0.38 | 0.73 | 24 | empty |
| 4 | 78 | 0.34 | 0.75 | 18 | empty |
| 5 | 57 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 4RMF · Biochemical and structural characterization of mycobacterial aspartyl-tRNA synthetase… · the same entry in another collection · chain A against A, TM-score 1.00
- A0QWN3 · AlphaFold monomer V2.0 prediction for aspartate--TRNA(ASP/ASN) ligase (A0QWN3) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 A0QWN3
- Elsewhere: RCSB PDB 4RMF · PDBe 4RMF · UniProt A0QWN3
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