1r54

X-ray diffraction
1.85Å resolution

Crystal structure of the catalytic domain of human ADAM33

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Disintegrin and metalloproteinase domain-containing protein 33 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.57 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q9BZ11 (Residues: 204-409; Coverage: 26%)
Gene names: ADAM33, C20orf153, UNQ873/PRO1891
Sequence domains: Reprolysin (M12B) family zinc metalloprotease
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: C2221
Unit cell:
a: 56.476Å b: 65.461Å c: 99.863Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.233
Expression system: Drosophila melanogaster