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1XJQ: 
ADP Complex OF HUMAN PAPS SYNTHETASE 1
Biological unit 1: dimeric
Source organism: Homo sapiens
Number of proteins:
2 (Bifunctional 3'-phosphoadenosine 5'-phosphosulf... ▼)
Protein molecule
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 Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
Number of chemicals:
3 (ADENOSINE-5'-DIPHOSPHATE (3) ▼)
Chemical
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ADENOSINE-5'-DIPHOSPHATE (3)
Similar Structures (471)help
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Showing 1 to 10 out of 471 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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Full
 1XNJ
APS complex of human PAPS synthetase 1
Homo sapiens
 2 0.28Å 1152 100%
2
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Full
 2QJF
Crystal structure of ATP-sulfurylase domain of human PAPS synthetase 1
Homo sapiens
 2 0.99Å 781 99%
3
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Full
 4MAF
Soybean ATP Sulfurylase
Glycine max
 2 1.06Å 763 59%
4
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Partial
 1JEE
Crystal Structure of ATP Sulfurylase in complex with chlorate
Saccharomyces cerevisiae
 1 2.11Å 378 24%
5
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Partial
 1I2D
CRYSTAL STRUCTURE OF ATP SULFURYLASE FROM PENICILLIUM CHRYSOGENUM
Penicillium chrysogenum
 1 2.04Å 377 26%
6
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Partial
 1G8H
ATP SULFURYLASE FROM S. CEREVISIAE: THE TERNARY PRODUCT COMPLEX WITH APS AND PPI
Saccharomyces cerevisiae
 1 2.03Å 376 25%
7
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Partial
 1G8G
ATP SULFURYLASE FROM S. CEREVISIAE: THE BINARY PRODUCT COMPLEX WITH APS
Saccharomyces cerevisiae
 1 2.03Å 376 25%
8
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Partial
 1JED
Crystal Structure of ATP Sulfurylase in complex with ADP
Saccharomyces cerevisiae
 1 2.09Å 376 25%
9
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Partial
 1J70
CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE
Saccharomyces cerevisiae
 1 2.16Å 376 24%
10
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Partial
 1JHD
Crystal Structure of Bacterial ATP Sulfurylase from the Riftia pachyptila Symbiont
sulfur-oxidizing endosymbiont of Riftia pachyptila
 1 2.88Å 376 23%
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{"1":"Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1","2":"Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1"}
Citing VAST
Gibrat JF, Madej T, Bryant SH. "Surprising similarities in structure comparison.", Curr Opin Struct Biol.1996 Jun;6(3):377-85
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. "MMDB and VAST+: tracking structural similarities between macromolecular complexes." Nucl. Acids Res. 2014 Jan;42(Database issue):D297-303
Thomas Madej, Aron Marchler-Bauer, Christopher Lanczycki, Dachuan Zhang, Stephen H Bryant "Biological Assembly Comparison With VAST" Methods Mol. Biol. 2020(2112):175-186
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?Original VAST
Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.