Structure analysis

Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2

X-ray diffraction
2.596Å resolution
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 22952.64 Å2
Buried surface area: 3907.59 Å2
Dissociation area: 1,118.62 Å2
Dissociation energy (ΔGdiss): 3.76 kcal/mol
Dissociation entropy (TΔSdiss): 11.06 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-142974

Macromolecules

Chain: A
Length: 542 amino acids
Theoretical weight: 59.45 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P22303 (Residues: 33-574; Coverage: 93%)
Gene name: ACHE
Pfam: Carboxylesterase family
InterPro:
CATH: alpha/beta hydrolase
PDBe-KB: UniProt Coverage View: P22303  
154250100150200250300350400450500
 
200400
UniProt
P22303
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces

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Chain: B
Length: 61 amino acids
Theoretical weight: 6.77 KDa
Source organism: Dendroaspis angusticeps
UniProt:
  • Canonical: P0C1Z0 (Residues: 1-61; Coverage: 100%)
Pfam: Snake toxin cobra-type
InterPro:
CATH: CD59
PDBe-KB: UniProt Coverage View: P0C1Z0  
16151015202530354045505560
 
204060TMCYSHTTTSRAILTNCGENSCYRKSRRHPPKMVLGRGCGCPPGDDNLEVKCCTSPDKCNY
UniProt
P0C1Z0
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces

Search similar proteins