› 6a0e

X-ray diffraction
1.95Å resolution

Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1)

Released:
DOI: 10.2210/pdb6a0e/pdb
PDB entry 6a0e coloured by chain, front view.
PDB entry 6a0e coloured by chain, side view.
PDB entry 6a0e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Analyses on the Deamidation of N-Terminal Asn in the Human N-Degron Pathway.
Park JS, Lee JY, Nguyen YTK, Kang NW, Oh EK, Jang DM, Kim HJ, Kim DD, Han BW
Biomolecules 10 (2020)
PMID: 31968674

Function and Biology Details

Reaction catalysed: 
N-terminal L-asparaginyl-[protein] + H(2)O = N-terminal L-aspartyl-[protein] + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein N-terminal asparagine amidohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 35.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96AB6 (Residues: 1-310; Coverage: 100%)
Gene name: NTAN1
Sequence domains: Protein N-terminal asparagine amidohydrolase

Ligands and Environments

2 bound ligands:
Ligand GOL 5 x GOL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P212121
Unit cell:
a: 83.153Å b: 84.903Å c: 87.198Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.224
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling.
Oh et al. (2020)
5 more

3 mentions without citation

Structural Analyses on the Deamidation of N-Terminal Asn in the Human N-Degron Pathway.
Park et al. (2020)
2 more