MolNFT v1 · #111729 · protein
Structure of the arabidopsis TAP38/PPH1, a state-transition phosphatase responsible for dephosphorylation of lhcii
4YZG · Protein phosphatase 2C 57: “Structure of the arabidopsis TAP38/PPH1, a state-transition phosphatase responsible for dephosphorylation of…”. X-ray diffraction, 2 ligands (MN, SO4), 7 pockets (best druggability 0.60). MolNFT v1…
- PDB
- 4YZG
- Type
- protein
- Length
- 588 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein phosphatase 2C 57
- EC
- 3.1.3.16
- UniProt
- P49599
- Ligands
- MN, SO4
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein phosphatase 2C 57 (EC 3.1.3.16) | protein | 294 | 37% helix, 28% strand | P49599 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 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 | 502 | 0.60 | 0.74 | 38 | empty |
| 2 | 163 | 0.53 | 0.80 | 21 | empty |
| 3 | 79 | 0.50 | 0.84 | 18 | empty |
| 4 | 64 | 0.42 | 0.81 | 16 | empty |
| 5 | 124 | 0.41 | 0.76 | 23 | MN, SO4 |
Interfaces
1 interface between chains.
- A–B · 640 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4YZG · Structure of the Arabidopsis TAP38/PPH1, a state-transition phosphatase responsible for… · the same entry in another collection · chain A against A, TM-score 1.00
- P49599 · AlphaFold monomer V2.0 prediction for protein phosphatase 2C 57 (P49599) · 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 P49599
- Elsewhere: RCSB PDB 4YZG · PDBe 4YZG · UniProt P49599
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