PDBe 4uhy

X-ray diffraction
3.2Å resolution

Crystal structure of the human RGMA-BMP2 complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bone morphogenetic protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12643 (Residues: 283-396; Coverage: 31%)
Gene names: BMP2, BMP2A
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines
Repulsive guidance molecule A Chain: C
Molecule details ›
Chain: C
Length: 106 amino acids
Theoretical weight: 11.63 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q96B86 (Residues: 46-139; Coverage: 23%)
Gene names: RGM, RGMA

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P3221
Unit cell:
a: 83.855Å b: 83.855Å c: 114.843Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.227 0.264
Expression systems:
  • Escherichia coli BL21(DE3)
  • Homo sapiens