› 3ljt

X-ray diffraction
1.6Å resolution

Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound

Released:
DOI: 10.2210/pdb3ljt/pdb
PDB entry 3ljt coloured by chain, front view.
PDB entry 3ljt coloured by chain, side view.
PDB entry 3ljt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure analysis reveals the flexibility of the ADAMTS-5 active site.
Shieh HS, Tomasselli AG, Mathis KJ, Schnute ME, Woodard SS, Caspers N, Williams JM, Kiefer JR, Munie G, Wittwer A, Malfait AM, Tortorella MD
Protein Sci 20 735-44 (2011)
PMID: 21370305

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
A disintegrin and metalloproteinase with thrombospondin motifs 5 Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 24.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNA0 (Residues: 264-480; Coverage: 24%)
Gene names: ADAMTS11, ADAMTS5, ADMP2
Sequence domains: Reprolysin (M12B) family zinc metalloprotease
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

4 bound ligands:
Ligand LA3 1 x LA3
Ligand EDO 1 x EDO
Ligand ZN 1 x ZN
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 51.398Å b: 44.518Å c: 76.251Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.198
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Emerging roles for ADAMTS5 during development and disease.
Kintakas et al. (2011)
1 more

3 mentions without citation

Crystal structure and substrate-induced activation of ADAMTS13.
Petri et al. (2019)
2 more