Research workbench
Crystal structure of the fha domain of human polynucleotide kinase 3' phosphatase
Analyse Crystal structure of the fha domain of human polynucleotide kinase 3'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BRF
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional polynucleotide PHOSPHATASE/KINASE
- EC
- 3.1.3.32, 2.7.1.78
- UniProt
- Q96T60
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional polynucleotide PHOSPHATASE/KINASE (EC 3.1.3.32, 2.7.1.78) | protein | 100 | 0% helix, 46% strand | Q96T60 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2BRF · Crystal Structure of the FHA Domain of Human Polynucleotide Kinase 3' Phosphatase · the same entry in another collection · chain A against A, TM-score 1.00
- Q96T60 · AlphaFold monomer V2.0 prediction for bifunctional polynucleotide PHOSPHATASE/KINASE… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q96T60
- Elsewhere: RCSB PDB 2BRF · PDBe 2BRF · UniProt Q96T60
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