Research workbench
ROP2 from toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity.
Analyse ROP2 from toxoplasma gondii: a virulence factor with a protein-kinase fold and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W1Z
- Type
- protein
- Length
- 712 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ROP2
- EC
- 2.7.-.-
- UniProt
- Q27007
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ROP2 (EC 2.7.-.-) | protein | 354 | 44% helix, 20% strand | Q27007 |
| B | ROP2 (EC 2.7.-.-) | protein | 358 | 44% helix, 21% strand | Q27007 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.71 | 0.76 | 75 | empty |
| 2 | 308 | 0.61 | 0.78 | 43 | empty |
| 3 | 284 | 0.58 | 0.78 | 40 | empty |
| 4 | 139 | 0.41 | 0.74 | 28 | empty |
| 5 | 69 | 0.39 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 279 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2W1Z · ROP2 from Toxoplasma gondii: A virulence factor with a protein- kinase fold and no… · 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 Q27007
- Elsewhere: RCSB PDB 2W1Z · PDBe 2W1Z · UniProt Q27007
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