Research workbench
Crystal structure of PFPK7 in complex with an ATP analogue
Analyse Crystal structure of PFPK7 in complex with an ATP analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PML
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SER/THR protein kinase
- UniProt
- Q7YTF7
- Ligands
- ANP, MN
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | SER/THR protein kinase | protein | 340 | 33% helix, 21% strand | Q7YTF7 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains X
- MN · Manganese (II) ion · metal · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.73 | 0.78 | 78 | MN, ANP |
| 2 | 87 | 0.38 | 0.76 | 15 | empty |
| 3 | 51 | 0.28 | 0.74 | 11 | empty |
Compared structures
- 2PML · Crystal structure of PfPK7 in complex with an ATP analogue · the same entry in another collection · chain X against X, 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 Q7YTF7
- Elsewhere: RCSB PDB 2PML · PDBe 2PML · UniProt Q7YTF7
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