MolNFT v1 · #85088 · protein

Human mitochondrial endo-exonuclease

4A1N · Nuclease exog, mitochondrial: “Human mitochondrial endo-exonuclease”. X-ray diffraction, 3 ligands (MG, NA, CL), 1 pocket (best druggability 0.52). MolNFT v1 #85088 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4A1N
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclease exog, mitochondrial
EC: 3.1.30.-
UniProt: Q9Y2C4
Ligands: MG, NA, CL
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclease exog, mitochondrial (EC 3.1.30.-)	protein	290	27% helix, 23% strand	Q9Y2C4

Ligands and binding sites

MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · chains A
CL · Chloride 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.52	0.74	39	MG, CL

Compared structures

4A1N · Human Mitochondrial endo-exonuclease · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y2C4 · AlphaFold monomer V2.0 prediction for nuclease exog, mitochondrial (Q9Y2C4) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9Y2C4
Elsewhere: RCSB PDB 4A1N · PDBe 4A1N · UniProt Q9Y2C4

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