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X-ray crystal structure of the DNA ligase III-alpha brct domain.

Analyse X-ray crystal structure of the DNA ligase III-alpha brct domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PC7
Type: protein
Length: 158 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA ligase 3
EC: 6.5.1.1
UniProt: P49916
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA ligase 3 (EC 6.5.1.1)	protein	81	32% helix, 12% strand	P49916
B	DNA ligase 3 (EC 6.5.1.1)	protein	77	34% helix, 10% strand	P49916

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.41	0.79	17	empty
2	62	0.39	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 206 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

3PC7 · X-ray crystal structure of the DNA ligase III-alpha BRCT domain. · the same entry in another collection · chain A against A, TM-score 1.00
P49916 · AlphaFold monomer V2.0 prediction for DNA ligase 3 (P49916) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P49916
Elsewhere: RCSB PDB 3PC7 · PDBe 3PC7 · UniProt P49916

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