4dd8

X-ray diffraction
2.1Å resolution

ADAM-8 metalloproteinase domain with bound batimastat

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human ADAM-8 catalytic domain complexed with batimastat.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 616-21 (2012)
PMID: 22684055

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160243 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disintegrin and metalloproteinase domain-containing protein 8 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 208 amino acids
Theoretical weight: 23.35 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P78325 (Residues: 196-403; Coverage: 26%)
Gene names: ADAM8, MS2
Sequence domains: Reprolysin (M12B) family zinc metalloprotease
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 91.6Å b: 50.9Å c: 93.5Å
α: 90° β: 102.4° γ: 90°
R-values:
R R work R free
0.192 0.188 0.255
Expression system: Homo sapiens