MolNFT v1 · #127984 · protein
OH1 from the orf virus: a tyrosine phosphatase that displays distinct structural features and triple substrate specificity
5NCR: “OH1 from the orf virus: a tyrosine phosphatase that displays distinct structural features and triple…”. X-ray diffraction, 2 ligands (PO4, SO4). MolNFT v1 #127984 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NCR
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6TW43
- Ligands
- PO4, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 173 | — | Q6TW43 |
| B | — | protein | 174 | — | Q6TW43 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NCR · OH1 from the Orf virus: a tyrosine phosphatase that displays distinct structural features… · 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 Q6TW43
- Elsewhere: RCSB PDB 5NCR · PDBe 5NCR · UniProt Q6TW43
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