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Structure and mechanism of T4 polynucleotide kinase

Analyse Structure and mechanism 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: 1LY1
Type: protein
Length: 152 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: SO4
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polynucleotide kinase (EC 2.7.1.78)	protein	152	53% helix, 13% strand	P06855

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	351	0.61	0.77	35	SO4

Compared structures

1LY1 · Structure and Mechanism 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 1LY1 · PDBe 1LY1 · UniProt P06855

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