MolNFT v2 · #129860 · protein
Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D
5OKP: “Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D”. X-ray diffraction at 1.85. MolNFT v2 #129860 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OKP
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Homo sapiens
- UniProt
- O15357
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 421 | — | O15357 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OKP · Crystal structure of human SHIP2 phosphatase-C2 double mutant F593D/L597D · 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 O15357
- Elsewhere: RCSB PDB 5OKP · PDBe 5OKP · UniProt O15357
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