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ATP dependent DNA ligase from S. solfataricus bound to ATP

Analyse ATP dependent DNA ligase from S. solfataricus bound to ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HIX
Type: protein
Length: 577 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermostable DNA ligase
EC: 6.5.1.1
UniProt: Q980T8
Ligands: ATP
Pockets: 5 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thermostable DNA ligase (EC 6.5.1.1)	protein	577	40% helix, 23% strand	Q980T8

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	204	0.60	0.81	34	ATP
2	82	0.46	0.81	18	empty
3	112	0.44	0.78	18	empty
4	90	0.42	0.79	16	empty
5	56	0.32	0.77	17	empty

Compared structures

2HIX · ATP dependent DNA ligase from S. solfataricus bound to ATP · the same entry in another collection · chain A against A, TM-score 1.00
Q980T8 · AlphaFold monomer V2.0 prediction for DNA ligase (Q980T8) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 Q980T8
Elsewhere: RCSB PDB 2HIX · PDBe 2HIX · UniProt Q980T8

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