MolNFT v1 · #21454 · protein
Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima
1SAZ · Probable butyrate kinase 2: “Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from…”. X-ray diffraction, 2 ligands (ACP, NA), 2 pockets (best druggability 0.65). MolNFT v1…
- PDB
- 1SAZ
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable butyrate kinase 2
- EC
- 2.7.2.7
- UniProt
- Q9X278
- Ligands
- ACP, NA
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable butyrate kinase 2 (EC 2.7.2.7) | protein | 375 | 44% helix, 19% strand | Q9X278 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- NA · Sodium ion · metal · chains A
- FMT · Formic acid · additive · 4 copies · 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 | 483 | 0.65 | 0.77 | 84 | FMT |
| 2 | 196 | 0.47 | 0.74 | 28 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1SAZ · Membership in the ASKHA Superfamily: Enzymological Properties and Crystal Structure of… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X278 · AlphaFold monomer V2.0 prediction for probable butyrate kinase 2 (Q9X278) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9X278
- Elsewhere: RCSB PDB 1SAZ · PDBe 1SAZ · UniProt Q9X278
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