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1PL4: 
Crystal Structure of human MnSOD Y166F mutant
Biological unit 1: tetrameric
Source organism: Homo sapiens
Number of proteins:
4 (Superoxide dismutase [Mn], mitochondrial ▼)
Protein molecule
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 Superoxide dismutase [Mn], mitochondrial
Number of chemicals:
4 (MANGANESE (II) ION (4) ▼)
Chemical
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MANGANESE (II) ION (4)
Similar Structures (156)help
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Showing 1 to 10 out of 156 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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 2P4K
Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Superoxide Dismutase
Homo sapiens
 4 0.18Å 788 98%
2
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 1ZTE
Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Suerpoxide Dismutase
Homo sapiens
 4 0.19Å 788 98%
3
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 2GDS
Interrupting the Hydrogen Bonding Network at the Active Site of Human Manganese Superoxide Dismutase
Homo sapiens
 4 0.27Å 788 98%
4
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 1ZSP
Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Superoxide Dismutase
Homo sapiens
 4 0.32Å 788 98%
5
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 1N0N
Catalytic and Structural Effects of Amino-Acid Substitution at His30 in Human Manganese Superoxide Dismutase
Homo sapiens
 4 0.32Å 788 98%
6
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 1XDC
Hydrogen Bonding in Human Manganese Superoxide Dismutase containing 3-Fluorotyrosine
Homo sapiens
 4 0.34Å 788 95%
7
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 1XIL
HYDROGEN BONDING IN HUMAN MANGANESE SUPEROXIDE DISMUTASE CONTAINING 3-FLUOROTYROSINE
Homo sapiens
 4 0.35Å 788 95%
8
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 1SZX
Role Of Hydrogen Bonding In The Active Site Of Human Manganese Superoxide Dismutase
Homo sapiens
 4 0.35Å 788 98%
9
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 5VF9
Native human manganese superoxide dismutase
Homo sapiens
 4 0.36Å 788 99%
10
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 1LUV
CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS 30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE: INSERTION OF VAL CGAMMA INTO THE SUBSTRATE ACCESS CHANNEL
Homo sapiens
 4 0.37Å 788 99%
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{"1":"Superoxide dismutase [Mn], mitochondrial","2":"Superoxide dismutase [Mn], mitochondrial","3":"Superoxide dismutase [Mn], mitochondrial","4":"Superoxide dismutase [Mn], mitochondrial"}
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.