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Crystal structure of T4 polynucleotide kinase
Analyse Crystal structure of T4 polynucleotide kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LTQ
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polynucleotide kinase
- EC
- 2.7.1.78
- UniProt
- P06855
- Ligands
- ADP
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polynucleotide kinase (EC 2.7.1.78) | protein | 298 | 44% helix, 16% strand | P06855 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 339 | 0.56 | 0.76 | 40 | ADP |
| 2 | 168 | 0.51 | 0.79 | 23 | empty |
| 3 | 80 | 0.34 | 0.75 | 15 | empty |
| 4 | 59 | 0.28 | 0.73 | 12 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1LTQ · Crystal structure of T4 polynucleotide kinase · 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 1LTQ · PDBe 1LTQ · UniProt P06855
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