Research workbench
Crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, new york structural genomics consortium
Analyse Crystal structure of mouse putative dual specificity phosphatase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HCM
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase
- UniProt
- Q8BTR5
- Ligands
- ZN, NA, WO4
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase | protein | 159 | 43% helix, 16% strand | Q8BTR5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- WO4 · Tungstate(vi)ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2HCM · Crystal structure of mouse putative dual specificity phosphatase complexed with zinc… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BTR5 · AlphaFold monomer V2.0 prediction for dual specificity phosphatase 28 (Q8BTR5) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q8BTR5
- Elsewhere: RCSB PDB 2HCM · PDBe 2HCM · UniProt Q8BTR5
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