Structure analysis

Crystal structure of QD-hNTAQ1 C28S

X-ray diffraction
1.46Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10779.74 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-188528
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 10670.28 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-188528

Macromolecules

Chains: A, B
Length: 204 amino acids
Theoretical weight: 23.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96HA8 (Residues: 1-202; Coverage: 99%)
Gene names: C8orf32, NTAQ1, WDYHV1
Pfam: N-terminal glutamine amidase

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