Research workbench
Selenomethionine substituted N-acetyl-L-glutamate kinase from escherichia COLI complexed with its substrate N-acetyl-L-glutamate and its substrate analog amppnp
Analyse Selenomethionine substituted N-acetyl-L-glutamate kinase from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GSJ
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylglutamate kinase
- EC
- 2.7.2.8
- UniProt
- P11445
- Ligands
- NLG, ANP, MG
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylglutamate kinase (EC 2.7.2.8) | protein | 258 | 43% helix, 23% strand | P11445 |
Ligands and binding sites
- NLG · N-acetyl-L-glutamate · ligand · chains A
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.65 | 0.81 | 39 | NLG, ANP, MG |
| 2 | 73 | 0.35 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1GSJ · Selenomethionine substituted N-acetyl-L-glutamate kinase from Escherichia coli complexed… · 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 P11445
- Elsewhere: RCSB PDB 1GSJ · PDBe 1GSJ · UniProt P11445
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