Research workbench
Crystal structure of a tetrameric acetylglutamate kinase from saccharomyces cerevisiae
Analyse Crystal structure of a tetrameric acetylglutamate kinase from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZZI
- Type
- protein
- Length
- 3,488 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylglutamate kinase
- EC
- 2.7.2.8
- UniProt
- Q01217
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Acetylglutamate kinase (EC 2.7.2.8) | protein | 436 | 40% helix, 24% strand | Q01217 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.77 | 0.86 | 48 | empty |
| 2 | 1022 | 0.76 | 0.79 | 90 | empty |
| 3 | 540 | 0.76 | 0.83 | 61 | empty |
| 4 | 689 | 0.72 | 0.79 | 76 | empty |
| 5 | 663 | 0.71 | 0.79 | 68 | empty |
Interfaces
14 interfaces between chains.
- E–H · 1622 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1594 Ų buried · 12 hydrogen bonds · protein-protein
- F–G · 1582 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1581 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1141 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3ZZI · Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae · the same entry in another collection · chain H against H, TM-score 1.00
- Q01217 · AlphaFold monomer V2.0 prediction for protein ARG5,6, mitochondrial (Q01217) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 Q01217
- Elsewhere: RCSB PDB 3ZZI · PDBe 3ZZI · UniProt Q01217
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