Research workbench
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition
Analyse The crystal structure of a phosphorylase kinase peptide substrate complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PHK
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphorylase kinase; Mc-peptide
- EC
- 2.7.1.38
- UniProt
- P00518
- Ligands
- ATP, MN
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphorylase kinase (EC 2.7.1.38) | protein | 277 | 39% helix, 19% strand | P00518 |
| B | Mc-peptide | protein | 7 | 0% helix, 29% strand | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.76 | 0.85 | 46 | MN, ATP |
| 2 | 85 | 0.41 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 659 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2PHK · The crystal structure of a phosphorylase kinase peptide substrate complex: kinase… · the same entry in another collection · chain A against A, TM-score 1.00
- P00518 · AlphaFold monomer V2.0 prediction for phosphorylase B kinase gamma catalytic chain… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P00518
- Elsewhere: RCSB PDB 2PHK · PDBe 2PHK · UniProt P00518
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