Structure analysis

Crystal structure of (+)-ABA-bound PYL1

X-ray diffraction
2.05Å resolution
Source organism: Arabidopsis thaliana
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9399.97 Ã…2
Buried surface area: 0.0 Ã…2
Dissociation area: 0 Ã…2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-186652
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9226.1 Ã…2
Buried surface area: 0.0 Ã…2
Dissociation area: 0 Ã…2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-186652
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 8889.11 Ã…2
Buried surface area: 0.0 Ã…2
Dissociation area: 0 Ã…2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-186652

Macromolecules

Chains: A, B, C
Length: 208 amino acids
Theoretical weight: 23.97 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VZS8 (Residues: 8-211; Coverage: 92%)
Gene names: At5g46790, MZA15.21, PYL1, RCAR12
Pfam: Polyketide cyclase / dehydrase and lipid transport
InterPro:
CATH: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

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