MolNFT v2 · #136931 · protein
Structure of T4Pnkp 3' phosphatase covalently bound to BeF3
5UJ0: “Structure of T4Pnkp 3' phosphatase covalently bound to BeF3”. X-ray diffraction at 2.3, 1 ligand (MG). MolNFT v2 #136931 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UJ0
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Enterobacteria phage T4
- UniProt
- P06855
- Ligands
- MG
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 143 | — | P06855 |
| B | — | protein | 142 | — | P06855 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UJ0 · Structure of T4PNKP 3' phosphatase covalently bound to BEF3 · 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 P06855
- Elsewhere: RCSB PDB 5UJ0 · PDBe 5UJ0 · UniProt P06855
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