Research workbench
Crystal structure of guanylate kinase from Plasmodium falciparum
Analyse Crystal structure of guanylate kinase from Plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z6G
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.18
- Source
- Plasmodium falciparum
- Molecule
- guanylate kinase
- EC
- 2.7.4.8
- UniProt
- Q8I2M1
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · resolution 2.18 · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | guanylate kinase (EC 2.7.4.8) | protein | 191 | 42% helix, 22% strand | Q8I2M1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 473 | 0.67 | 0.78 | 38 | SO4, EPE |
Compared structures
- 1Z6G · Crystal structure of guanylate kinase from plasmodium falciparum · 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 Q8I2M1
- Elsewhere: RCSB PDB 1Z6G · PDBe 1Z6G · UniProt Q8I2M1
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