Research workbench
Crystal structure of the human pnkp fha domain in complex with an XRCC1-derived phosphopeptide
Analyse Crystal structure of the human pnkp fha domain in complex with an XRCC1-derived… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W3O
- Type
- protein
- Length
- 217 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional polynucleotide PHOSPHATASE/KINASE; DNA repair protein XRCC1
- EC
- 3.1.3.32, 2.7.1.78
- UniProt
- Q96T60, P18887
- Ligands
- CA
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 45% 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 |
| B | Bifunctional polynucleotide PHOSPHATASE/KINASE (EC 3.1.3.32, 2.7.1.78) | protein | 101 | 0% helix, 48% strand | Q96T60 |
| C, D | DNA repair protein XRCC1 | protein | 8 | 0% helix, 0% strand | P18887 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–D · 580 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 576 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 84 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 2W3O · Crystal structure of the human PNKP FHA domain in complex with an XRCC1-derived… · 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
- P18887 · AlphaFold monomer V2.0 prediction for DNA repair protein XRCC1 (P18887) · a predicted model of the same protein · chain C against A, TM-score 0.54
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
- Every structure of UniProt P18887
- Elsewhere: RCSB PDB 2W3O · PDBe 2W3O · UniProt Q96T60 · UniProt P18887
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