Research workbench

Human aprataxin (aptx) bound to nicked RNA-DNA, AMP and zn product complex

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

PDB: 6CVO
Type: protein + DNA
Length: 409 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q7Z2E3
Ligands: AMP, ZN

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	175	—	Q7Z2E3
D, G	—	dna	22	—	—
B	—	protein	178	—	Q7Z2E3
E, H	—	dna	6	—	—

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, D, B, G

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

Compared structures

6CVO · Human Aprataxin (Aptx) bound to nicked RNA-DNA, AMP and Zn product complex · 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 A 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 6CVO · PDBe 6CVO · UniProt Q7Z2E3

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