› 2pez

X-ray diffraction
1.4Å resolution

Crystal structrue of deletion mutant of APS-kinase domain of human PAPS-synthetase 1 in complex with cyclic PAPS and dADP

Released:
DOI: 10.2210/pdb2pez/pdb
PDB entry 2pez coloured by chain, front view.
PDB entry 2pez coloured by chain, side view.
PDB entry 2pez coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation.
Sekulic N, Konrad M, Lavie A
J Biol Chem 282 22112-21 (2007)
PMID: 17540769

Function and Biology Details

Reactions catalysed: 
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
ATP + sulfate = diphosphate + adenylyl sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 179 amino acids
Theoretical weight: 19.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43252 (Residues: 51-226; Coverage: 28%)
Gene names: ATPSK1, PAPSS, PAPSS1
Sequence domains: Adenylylsulphate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand GGZ 1 x GGZ
Ligand DAT 2 x DAT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 44.09Å b: 59.4Å c: 139.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.22
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Adenosine-5'-phosphosulfate--a multifaceted modulator of bifunctional 3'-phospho-adenosine-5'-phosphosulfate synthases and related enzymes.
Mueller et al. (2013)
8 other articles

3 mentions without citation

Predicting new indications for approved drugs using a proteochemometric method.
Dakshanamurthy et al. (2012)
2 more