Research workbench
Crystal structure of dual specificity protein phosphatase 23 from homo sapiens in complex with ligand malate ion
Analyse Crystal structure of dual specificity protein phosphatase 23 from homo sapiens… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IMG
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase 23
- EC
- 3.1.3.48, 3.1.3.16
- UniProt
- Q9BVJ7
- Ligands
- MLT
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase 23 (EC 3.1.3.48, 3.1.3.16) | protein | 149 | 44% helix, 15% strand | Q9BVJ7 |
Ligands and binding sites
- MLT · D-malate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 2IMG · Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BVJ7 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 23 (Q9BVJ7) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9BVJ7
- Elsewhere: RCSB PDB 2IMG · PDBe 2IMG · UniProt Q9BVJ7
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