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Crystal structure of the dbd domain of human DNA ligase IV apo form

Analyse Crystal structure of the dbd domain of human DNA ligase IV apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HTO
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA ligase 4
EC: 6.5.1.1
UniProt: P49917
Ligands: PO4
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA ligase 4 (EC 6.5.1.1)	protein	214	64% helix, 2% strand	P49917

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.37	0.80	11	empty

Compared structures

4HTO · Crystal structure of the DBD domain of human DNA ligase IV Apo form · the same entry in another collection · chain A against A, TM-score 1.00
P49917 · AlphaFold monomer V2.0 prediction for DNA ligase 4 (P49917) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P49917
Elsewhere: RCSB PDB 4HTO · PDBe 4HTO · UniProt P49917

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