Research workbench
Crystal structure of possible 1-phosphofructokinase (ec 2.7.1.56) (TM0828) from thermotoga maritima at 2.46 a resolution
Analyse Crystal structure of possible 1-phosphofructokinase (ec 2.7.1.56) (TM0828) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AJR
- Type
- protein
- Length
- 640 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar kinase, pfkb family
- UniProt
- Q9WZT5
- Ligands
- MG
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sugar kinase, pfkb family | protein | 320 | 37% helix, 27% strand | Q9WZT5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 805 | 0.78 | 0.81 | 78 | ACT |
| 2 | 838 | 0.76 | 0.80 | 71 | ACT |
| 3 | 219 | 0.57 | 0.79 | 26 | empty |
| 4 | 188 | 0.50 | 0.77 | 29 | empty |
| 5 | 89 | 0.38 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1639 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2AJR · Crystal structure of Possible 1-phosphofructokinase (EC 2.7.1.56) (tm0828) from… · 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 Q9WZT5
- Elsewhere: RCSB PDB 2AJR · PDBe 2AJR · UniProt Q9WZT5
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