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Crystal structure of tryptophanyl-tRNA synthetase from bacillus stearothermophilus in complex with chuangxinmycin and ATP
Analyse Crystal structure of tryptophanyl-tRNA synthetase from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CKI
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00953
- Ligands
- 9E0, ATP, K, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | P00953 |
Ligands and binding sites
- 9E0 · (5~{S},6~{R})-5-methyl-7-thia-2-azatricyclo[6.3.1.0^{4, 12}]dodeca-1(12),3,8,10-tetraene-6-carboxylic acid · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- K · Potassium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CKI · Crystal structure of Tryptophanyl-tRNA synthetase from Bacillus stearothermophilus in… · 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 P00953
- Elsewhere: RCSB PDB 7CKI · PDBe 7CKI · UniProt P00953
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