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Crystal structure of the archaeal asparagine synthetase a complexed with L-aspartic acid and adenosine triphosphate
Analyse Crystal structure of the archaeal asparagine synthetase a complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3REU
- Type
- protein
- Length
- 584 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9V228
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 294 | — | Q9V228 |
| B | — | protein | 290 | — | Q9V228 |
Compared structures
- 3REU · Crystal structure of the archaeal asparagine synthetase A complexed with L-Aspartic acid… · 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 Q9V228
- Elsewhere: RCSB PDB 3REU · PDBe 3REU · UniProt Q9V228
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