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High resolution crystal structure of the vaccinia virus dual- specificity phosphatase VH1
Analyse High resolution crystal structure of the vaccinia virus dual- specificity… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CM3
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase
- EC
- 3.1.3.48, 3.1.3.-
- UniProt
- P07239
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase (EC 3.1.3.48, 3.1.3.-) | protein | 164 | 45% helix, 11% strand | P07239 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3CM3 · High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1 · 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 P07239
- Elsewhere: RCSB PDB 3CM3 · PDBe 3CM3 · UniProt P07239
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