Research workbench
KI67-PP1G (protein phosphatase 1, gamma isoform) holoenzyme complex
Analyse KI67-PP1G (protein phosphatase 1, gamma isoform) holoenzyme complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J28
- Type
- protein
- Length
- 652 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase PP1-gamma catalytic subunit; Antigen ki-67
- EC
- 3.1.3.16
- UniProt
- P36873, P46013
- Ligands
- NA
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE-protein phosphatase PP1-gamma catalytic subunit (EC 3.1.3.16) | protein | 293 | 35% helix, 21% strand | P36873 |
| C, D | Antigen ki-67 | protein | 33 | 0% helix, 18% strand | P46013 |
Ligands and binding sites
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 | 915 | 0.77 | 0.80 | 76 | MLI |
| 2 | 104 | 0.39 | 0.76 | 20 | empty |
| 3 | 83 | 0.37 | 0.76 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1298 Ų buried · 22 hydrogen bonds · protein-protein
- B–D · 1252 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 915 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5J28 · Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex · 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
- Every structure of UniProt P46013
- Elsewhere: RCSB PDB 5J28 · PDBe 5J28 · UniProt P36873 · UniProt P46013
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