› 4ust

X-ray diffraction
1.9Å resolution

Crystal structure of human soluble Adenylyl Cyclase with pyrophosphate resulting from soaking with GTP and Magnesium

Released:
DOI: 10.2210/pdb4ust/pdb
PDB entry 4ust coloured by chain, front view.
PDB entry 4ust coloured by chain, side view.
PDB entry 4ust coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of human soluble adenylyl cyclase and crystal structures of its nucleotide complexes-implications for cyclase catalysis and evolution.
Kleinboelting S, van den Heuvel J, Steegborn C
FEBS J 281 4151-64 (2014)
PMID: 25040695

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate cyclase type 10 Chain: A
Molecule details ›
Chain: A
Length: 475 amino acids
Theoretical weight: 54.27 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Best match: Q96PN6 (Residues: 1-469)
Gene names: ADCY10, SAC

Ligands and Environments

6 bound ligands:
Ligand MG 1 x MG
Ligand CL 2 x CL
Ligand POP 1 x POP
Ligand ACT 1 x ACT
Ligand EDO 2 x EDO
Ligand GOL 1 x GOL
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P63
Unit cell:
a: 100.34Å b: 100.34Å c: 97.42Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.161 0.202
Expression system: Trichoplusia ni

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Citations

3 review citations

International Union of Basic and Clinical Pharmacology. CI. Structures and Small Molecule Modulators of Mammalian Adenylyl Cyclases.
Dessauer et al. (2017)
2 more

1 mention without citation

Structural analysis of human soluble adenylyl cyclase and crystal structures of its nucleotide complexes-implications for cyclase catalysis and evolution.
Kleinboelting et al. (2014)