Research workbench
Crystal structure of the complex between calyculin a and the catalytic subunit of protein phosphatase 1
Analyse Crystal structure of the complex between calyculin a and the catalytic subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IT6
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE protein phosphatase 1 gamma (PP1-gamma) catalytic subunit
- EC
- 3.1.3.16
- UniProt
- P36873
- Ligands
- CYU, MN
- Pockets
- 5 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE protein phosphatase 1 gamma (PP1-gamma) catalytic subunit (EC 3.1.3.16) | protein | 293 | 34% helix, 19% strand | P36873 |
Ligands and binding sites
- CYU · Calyculin A · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.37 | 0.74 | 19 | empty |
| 2 | 73 | 0.37 | 0.77 | 16 | MN |
| 3 | 54 | 0.35 | 0.78 | 12 | empty |
| 4 | 92 | 0.34 | 0.74 | 19 | empty |
| 5 | 57 | 0.32 | 0.76 | 16 | empty |
Compared structures
- 1IT6 · Crystal structure of the complex between calyculin a and the catalytic subunit of protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P36873 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PP1-gamma… · a predicted model of the same protein · 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 P36873
- Elsewhere: RCSB PDB 1IT6 · PDBe 1IT6 · UniProt P36873
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