PDBe 3edh

X-ray diffraction
1.25Å resolution

Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO

Released:
Source organism: Homo sapiens
Entry author: Mac Sweeney A

Function and Biology Details

Reaction catalysed:
Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bone morphogenetic protein 1 Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13497 (Residues: 121-321; Coverage: 21%)
Gene names: BMP1, PCOLC
Sequence domains: Astacin (Peptidase family M12A)
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 53.499Å b: 59.093Å c: 69.451Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.14 0.172
Expression system: Escherichia coli