Structure analysis

Crystal structure of P-selectin lectin/EGF domains

X-ray diffraction
2.4Å resolution
Source organism: Homo sapiens
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 34287.27 Å2
Buried surface area: 2656.38 Å2
Dissociation area: 929.37 Å2
Dissociation energy (ΔGdiss): -32.64 kcal/mol
Dissociation entropy (TΔSdiss): 37.03 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147622

Macromolecules

Chains: A, B, C, D
Length: 162 amino acids
Theoretical weight: 19.13 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P16109 (Residues: 42-199; Coverage: 20%)
Gene names: GMRP, GRMP, SELP
Pfam: Lectin C-type domain
InterPro:
CATH:
SCOP:
PDBe-KB: UniProt Coverage View: P16109  
116220406080100120140160
 
50100150WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADNEPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGNYTCSCYPGFYGPECEYVRDDDDK
UniProt
P16109
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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