Research workbench
Crystal structure of trypanosoma cruzi glucokinase in the apo form (open conformation)
Analyse Crystal structure of trypanosoma cruzi glucokinase in the apo form (open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S2H
- Type
- protein
- Length
- 737 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucokinase 1, putative
- EC
- 2.7.1.2
- UniProt
- Q4E4E1
- Ligands
- NA, SO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucokinase 1, putative (EC 2.7.1.2) | protein | 369 | 43% helix, 24% strand | Q4E4E1 |
| B | Glucokinase 1, putative (EC 2.7.1.2) | protein | 368 | 43% helix, 24% strand | Q4E4E1 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.76 | 0.78 | 96 | empty |
| 2 | 53 | 0.73 | 0.99 | 23 | empty |
| 3 | 728 | 0.71 | 0.78 | 74 | SO4 |
| 4 | 50 | 0.42 | 0.83 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1809 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7S2H · Crystal structure of Trypanosoma cruzi glucokinase in the apo form (open conformation) · 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 Q4E4E1
- Elsewhere: RCSB PDB 7S2H · PDBe 7S2H · UniProt Q4E4E1
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