› 6a0i

X-ray diffraction
2Å resolution

Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant

Released:
DOI: 10.2210/pdb6a0i/pdb
PDB entry 6a0i coloured by chain, front view.
PDB entry 6a0i coloured by chain, side view.
PDB entry 6a0i 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: 35.78 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 22 x GOL
Ligand PO4 3 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: 82.982Å b: 84.34Å c: 86.998Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Tying up loose ends: the N-degron and C-degron pathways of protein degradation.
Timms et al. (2020)
6 other articles

1 mention without citation

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