Research workbench

Human aprataxin (aptx) L248M bound to DNA, AMP and zn product

Analyse Human aprataxin (aptx) L248M bound to DNA, AMP and zn product in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CVS
Type: protein + DNA
Length: 398 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q7Z2E3
Ligands: AMP, ZN

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	180	—	Q7Z2E3
B	—	protein	178	—	Q7Z2E3
D, E, G, H	—	dna	10	—	—

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 2 copies · chains A, D, B, G
ZN · Zinc ion · metal · 2 copies · chains A, B
BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B, D, G

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

Compared structures

6CVS · Human Aprataxin (Aptx) L248M bound to DNA, AMP and Zn product · the same entry in another collection · chain H against H, TM-score 1.00
Q7Z2E3 · AlphaFold monomer V2.0 prediction for aprataxin (Q7Z2E3) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q7Z2E3
Elsewhere: RCSB PDB 6CVS · PDBe 6CVS · UniProt Q7Z2E3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.