Research workbench
The regulatory subunit of aspartate kinase in complex with threonine from mycobacterium tuberculosis
Analyse The regulatory subunit of aspartate kinase in complex with threonine from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GO7
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartokinase
- EC
- 2.7.2.4
- UniProt
- P0A4Z8
- Ligands
- THR
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Aspartokinase (EC 2.7.2.4) | protein | 165 | 33% helix, 34% strand | P0A4Z8 |
Ligands and binding sites
- THR · Threonine · ligand · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4GO7 · The regulatory subunit of aspartate kinase in complex with threonine from Mycobacterium… · the same entry in another collection · chain X against X, 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 P0A4Z8
- Elsewhere: RCSB PDB 4GO7 · PDBe 4GO7 · UniProt P0A4Z8
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