X-ray diffraction
1.95Å resolution

Co-crystal structure of Rap1 in complex with KRIT1


Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Rap-1b Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P61224 (Residues: 1-167; Coverage: 91%)
Gene names: OK/SW-cl.11, RAP1B
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Krev interaction trapped protein 1 Chain: B
Molecule details ›
Chain: B
Length: 322 amino acids
Theoretical weight: 37.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O00522 (Residues: 420-736; Coverage: 43%)
Gene names: CCM1, KRIT1
Sequence domains: FERM central domain
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 57.548Å b: 77.97Å c: 59.757Å
α: 90° β: 90.93° γ: 90°
R R work R free
0.198 0.196 0.239
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21(DE3)