MolNFT v1 · #116082 · protein
Crystal structure of tppha variant - H39A
5D2U · Protein serin-threonin phosphatase: “Crystal structure of tppha variant - H39A”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.44). MolNFT v1 #116082 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5D2U
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein serin-threonin phosphatase
- UniProt
- Q8DGS1
- Ligands
- CA
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein serin-threonin phosphatase | protein | 240 | 32% helix, 28% strand | Q8DGS1 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.44 | 0.75 | 30 | CA |
Compared structures
- 5D2U · Crystal structure of tPphA Variant - H39A · the same entry in another collection · 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 Q8DGS1
- Elsewhere: RCSB PDB 5D2U · PDBe 5D2U · UniProt Q8DGS1
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