6a0f

X-ray diffraction
2.38Å resolution

Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Phe-Ala-Ala-Arg peptide

Released:

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-166390 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
5-mer peptide Asn-Phe-Ala-Ala-Arg Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 579 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P212121
Unit cell:
a: 84.045Å b: 85.749Å c: 88.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.248
Expression systems:
  • Escherichia coli BL21
  • Not provided