Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-191509 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
C-type lectin domain family 1 member B
Molecule details ›
Chains: C, F, I, L
Length: 128 amino acids
Theoretical weight: 15.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
Length: 128 amino acids
Theoretical weight: 15.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9P126 (Residues: 96-221; Coverage: 55%)
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec rhodocytin subunit alpha
Molecule details ›
Chains: A, D, G, J
Length: 136 amino acids
Theoretical weight: 15.81 KDa
Source organism: Calloselasma rhodostoma
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 136 amino acids
Theoretical weight: 15.81 KDa
Source organism: Calloselasma rhodostoma
UniProt:
- Canonical: Q9I841 (Residues: 1-136; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Snaclec rhodocytin subunit beta
Molecule details ›
Chains: B, E, H, K
Length: 146 amino acids
Theoretical weight: 16.79 KDa
Source organism: Calloselasma rhodostoma
UniProt:
Structure domains: Mannose-Binding Protein A, subunit A
Length: 146 amino acids
Theoretical weight: 16.79 KDa
Source organism: Calloselasma rhodostoma
UniProt:
- Canonical: Q9I840 (Residues: 1-146; Coverage: 100%)
Structure domains: Mannose-Binding Protein A, subunit A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-5A
Spacegroup:
C2
Expression system: Escherichia coli
