1MKA: Beta-hydroxydecanoyl thiol ester dehydrase

E. Coli beta-hydroxydecanoyl thiol ester dehydrase modified by its classic mechanism-based inactivator, 3-decynoyl-N-acetyl cysteamine. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Jul 1996.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Escherichia coli
Chains: 2
Atoms: 2,972
Mol. weight: 38.26 kDa
Ligands: DAC
Released: 11 Jul 1996

Explore 1MKA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MKA contains 8 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	1
α-helix	9-16	8
α-helix	28-30	3
β-strand	38-43	6	1
β-strand	53-59	7	1
α-helix	65-68	4
α-helix	79-96	18
β-strand	102-108	7	1
β-strand	111-113	3	1
β-strand	123-135	13	1
β-strand	139-149	11	1
β-strand	152-165	14	1

Chain B: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	1
α-helix	9-16	8
α-helix	28-30	3
β-strand	38-43	6	1
β-strand	53-59	7	1
α-helix	65-69	5
α-helix	79-96	18
β-strand	102-108	7	1
β-strand	110-113	4	1
β-strand	123-136	14	1
β-strand	138-149	12	1
β-strand	152-165	14	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-hydroxydecanoyl thiol ester dehydrase	A, B	protein	171	Escherichia coli	P0A6Q3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1MKA_1 BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE (chains A, B)
VDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELDI
NPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPT
AKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSAF

Ligands and cofactors

ID	Name	Formula	Copies
DAC	2-decenoyl N-acetyl cysteamine	C14 H25 N O2 S	2

Primary citation

Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Leesong, M., Henderson, B.S., Gillig, J.R. et al. Structure (1996) 4:253-264. DOI 10.1016/S0969-2126(96)00030-5 · PubMed

Other PDB entries of the same protein (UniProt P0A6Q3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4KEH 1.9 Å, Crosslinked Crystal Structure of Type II Fatty Synthase Dehydratase, FabA, and Acyl…
1MKB 2.0 Å, Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase at PH 5 and 21 degrees C

Browse structure collections

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