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4KE9: 
Crystal Structure Of Monoglyceride Lipase From Bacillus Sp. H257 In Complex With An 1-stearyol Glycerol Analogue
Biological unit 1: monomeric
Source organism: Bacillus sp. H-257
Number of proteins:
1 (THERMOSTABLE MONOACYLGLYCEROL LIPASE)
Number of chemicals:
1 (Hexadecyl Hydrogen (R)-(3-Azidopropyl)phosphonate ▼)
Chemical
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Hexadecyl Hydrogen (R)-(3-Azidopropyl)phosphonate
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      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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 4KE8
Crystal structure of Monoglyceride lipase from Bacillus sp. H257 in complex with monopalmitoyl glycerol analogue
Bacillus sp. H-257
 1 0.22Å 247 100%
2
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 4KEA
Crystal structure of D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in space group P212121
Bacillus sp. H-257
 1 0.95Å 246 97%
3
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 4LHE
Crystal structure of closed form of Monoacylglycerol Lipase
Bacillus sp. H-257
 1 1.13Å 246 100%
4
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 3RM3
Crystal structure of monoacylglycerol lipase from Bacillus sp. H257
Bacillus sp. H-257
 1 0.41Å 244 100%
5
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 4KE6
Crystal structure D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in complex with 1-rac-lauroyl glycerol
Bacillus sp. H-257
 1 0.93Å 244 99%
6
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 4KE7
Crystal Structure Of Monoglyceride Lipase From Bacillus Sp. H257 In Complex With An 1-myristoyl Glycerol Analogue
Bacillus sp. H-257
 1 0.43Å 242 100%
7
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 3RLI
Crystal structure of monoacylglycerol lipase from Bacillus sp. H257 in complex with PMSF
Bacillus sp. H-257
 1 0.40Å 241 100%
8
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 4FBM
LipS and LipT, two metagenome-derived lipolytic enzymes increase the diversity of known lipase and esterase families
Others
 1 1.12Å 240 50%
9
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 4FBL
LipS and LipT, two metagenome-derived lipolytic enzymes increase the diversity of known lipase and esterase families
Others
 1 0.89Å 234 51%
10
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 6AX1
Structure of human monoacylglycerol lipase bound to a covalent inhibitor
Homo sapiens
 1 2.41Å 230 17%
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{"1":"THERMOSTABLE MONOACYLGLYCEROL LIPASE"}
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 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.