Research workbench
Human VH1-related dual-specificity phosphatase
Analyse Human VH1-related dual-specificity phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VHR
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human VH1-related dual-specificity phosphatase vhr
- EC
- 3.1.3.48
- UniProt
- P51452
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Human VH1-related dual-specificity phosphatase vhr (EC 3.1.3.48) | protein | 178 | 44% helix, 13% strand | P51452 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P51452
- Elsewhere: RCSB PDB 1VHR · PDBe 1VHR · UniProt P51452
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