Research workbench
1.85 ångström crystal structure of putative sedoheptulose-1,7 bisphosphatase from toxoplasma gondii
Analyse 1.85 ångström crystal structure of putative sedoheptulose-1,7 bisphosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IR8
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sedoheptulose-1,7 bisphosphatase, putative
- EC
- 3.1.3.37
- UniProt
- B9PW60
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sedoheptulose-1,7 bisphosphatase, putative (EC 3.1.3.37) | protein | 310 | 37% helix, 23% strand | B9PW60 |
| B | Sedoheptulose-1,7 bisphosphatase, putative (EC 3.1.3.37) | protein | 324 | 35% helix, 26% strand | B9PW60 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.77 | 0.86 | 47 | empty |
| 2 | 318 | 0.59 | 0.77 | 38 | empty |
| 3 | 79 | 0.36 | 0.76 | 17 | empty |
| 4 | 51 | 0.28 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2259 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
- 4IR8 · 1.85 Angstrom Crystal Structure of Putative Sedoheptulose-1,7 bisphosphatase 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 B9PW60
- Elsewhere: RCSB PDB 4IR8 · PDBe 4IR8 · UniProt B9PW60
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.