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Structure of trprs II bound to ATP
Analyse Structure of trprs II bound to ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A4M
- Type
- protein
- Length
- 993 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophanyl-tRNA synthetase II
- EC
- 6.1.1.2
- UniProt
- Q9RVD6
- Ligands
- TRP
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Tryptophanyl-tRNA synthetase II (EC 6.1.1.2) | protein | 331 | 58% helix, 8% strand | Q9RVD6 |
Ligands and binding sites
- TRP · Tryptophan · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 772 | 0.80 | 0.83 | 64 | empty |
| 2 | 838 | 0.77 | 0.81 | 60 | TRP |
| 3 | 792 | 0.73 | 0.78 | 56 | empty |
| 4 | 53 | 0.30 | 0.75 | 19 | empty |
Interfaces
2 interfaces between chains.
- A–C · 2004 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 98 Ų buried · 1 hydrogen bond · 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 Q9RVD6
- Elsewhere: RCSB PDB 2A4M · PDBe 2A4M · UniProt Q9RVD6
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