MolNFT v1 · #5890 · protein
Crystal structure of a human phosphatase
1EW2: “Crystal structure of a human phosphatase”. X-ray diffraction, 4 ligands (NAG, ZN, MG), 3 pockets (best druggability 0.33). MolNFT v1 #5890 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EW2
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatase
- EC
- 3.1.3.1
- UniProt
- P05187
- Ligands
- NAG, ZN, MG, PO4
- Pockets
- 3 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatase (EC 3.1.3.1) | protein | 479 | 33% helix, 18% strand | P05187 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.33 | 0.78 | 16 | empty |
| 2 | 99 | 0.33 | 0.73 | 25 | PO4 |
| 3 | 69 | 0.33 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
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 P05187
- Elsewhere: RCSB PDB 1EW2 · PDBe 1EW2 · UniProt P05187
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