Structure for bestatin (M01.014 inhibitor)

Summary Structure Literature

 

PDB Organism Resolution Comment
1HS6_A Homo sapiens 1.95 Å complex with bestatin
The catalytic zinc is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His295 and His299 in purple, and Glu318 in dark blue. The catalytic Glu296 is also shown in ball-and-stick representation in dark blue. Bound bestatin is shown in grey in ball-and-stick representation.
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2XQ0 Saccharomyces cerevisiae 1.96 Å complex with bestatin
The catalytic zinc atom is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His340 and His344 in purple, and and Glu363 in dark blue. The catalytic residues are shown in ball-and-stick representation: Glu341 in blue and Tyr429 in green. The bound inhibitor bestatin is shown in grey ball-and-stick representation.
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2ZOG Mus musculus 1.70 Å complex with zinc and bestatin
The catalytic zinc atoms are shown as light grey CPK spheres. The zinc ligands are shown in ball-and-stick representation: His99 and His445 in purple, Asp132 and Asp195 in pink and Glu167 in blue. The catalytic residues are shown in ball-and-stick representation: Asp101 in pink and Glu166 in blue. The bound inhibitor is shown in grey ball-and-stick representation.
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3EBH_A Plasmodium falciparum 1.65 Å complex with bestatin
The catalytic zinc atom is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His496 in purple, His500 in purple and Glu519 in blue. The catalytic residues are shown in ball-and-stick representation: Glu497 in blue and Tyr580 in green. The bound inhibitor bestatin is shown in grey ball-and-stick representation.
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3MDJ Homo sapiens 2.95 Å complex with bestatin
The catalytic zinc atom is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His341 in purple, His345 in purple and Glu364 in blue. The catalytic residues are shown in ball-and-stick representation: Glu342 in blue and Tyr426 in green. The bound inhibitor bestatin is shown in grey ball-and-stick representation.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
alanyl aminopeptidase (bacterial-type) ( Escherichia coli)
complex with bestatin 1.60 Å 2DQM 2DQM 2DQM 2DQM 2DQM 2DQM Ito et al., 2006
complex with bestatin 2.30 Å 2HPT 2HPT 2HPT 2HPT 2HPT 2HPT Addlagatta et al., 2006
Met260Ala mutant; complex with bestatin 2.30 Å 4XMX 4XMX 4XMX 4XMX 4XMX 4XMX
aminopeptidase A/I (Helicobacter-type) ( Helicobacter pylori)
complex with bestatin 1.90 Å 4ZLA 4ZLA 4ZLA 4ZLA 4ZLA 4ZLA Modak et al., 2016
leukotriene A4 hydrolase ( Homo sapiens)
complex with bestatin 1.95 Å 1HS6 1HS6 1HS6 1HS6 1HS6 1HS6 Thunnissen et al., 2001
endoplasmic reticulum aminopeptidase 1 ( Homo sapiens)
complex with bestatin 2.95 Å 3MDJ 3MDJ 3MDJ 3MDJ 3MDJ 3MDJ Nguyen et al., 2011
aminopeptidase A ( Homo sapiens)
complex with bestatin 2.40 Å 4KXB 4KXB 4KXB 4KXB 4KXB 4KXB Yang et al., 2013
carnosine dipeptidase II ( Mus musculus)
complex with manganese and bestatin 2.30 Å 2ZOF 2ZOF 2ZOF 2ZOF 2ZOF 2ZOF Unno et al., 2008
complex with zinc and bestatin 1.70 Å 2ZOG 2ZOG 2ZOG 2ZOG 2ZOG 2ZOG Unno et al., 2008
M1 aminopeptidase (Plasmodium spp.) ( Plasmodium falciparum)
complex with bestatin 1.65 Å 3EBH 3EBH 3EBH 3EBH 3EBH 3EBH McGowan et al., 2009
PepA aminopeptidase ( Pseudomonas putida)
complex with bestatin 1.50 Å 3H8G 3H8G 3H8G 3H8G 3H8G 3H8G Kale et al., 2010
leukotriene A4 hydrolase (Saccharomyces cerevisiae) ( Saccharomyces cerevisiae)
complex with bestatin 1.96 Å 2XQ0 2XQ0 2XQ0 2XQ0 2XQ0 2XQ0 Helgstrand et al., 2011
LAPTc aminopeptidase ( Trypanosoma brucei)
complex with bestatin 2.30 Å 5NTD 5NTD 5NTD 5NTD 5NTD 5NTD
aminopeptidase Ap1 ( Vibrio proteolyticus)
complex with bestatin 2.00 Å 1TXR 1TXR 1TXR 1TXR 1TXR 1TXR Stamper et al., 2004
complex with bestatin 2.10 Å 1XRY 1XRY 1XRY 1XRY 1XRY 1XRY
leukotriene A4 hydrolase ( Xenopus laevis)
complex with inhibitor bestatin 2.26 Å 4GAA 4GAA 4GAA 4GAA 4GAA 4GAA