9MLW: 3-oxoacyl-[acyl-carrier-protein] synthase 1

Crosslinked complex of ketosynthase FabB mutant FabBG107M and acyl carrier protein AcpP from E.coli with C8 crosslinker. Determined by X-ray diffraction at 2.21 Å resolution. Released 18 Mar 2026.

Method: X-ray diffraction
Resolution: 2.21 Å
Organism: Escherichia coli
Chains: 4
Atoms: 7,375
Mol. weight: 103.36 kDa
Ligands: A1BMZ
Released: 18 Mar 2026

Explore 9MLW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9MLW contains 54 α-helices and 57 β-strands across 4 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: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
β-strand	13	1	2
β-strand	16	1	2
α-helix	19-28	10
β-strand	34-35	2	3
α-helix	37-42	6
β-strand	48-50	3	3
α-helix	62-65	4
α-helix	70-86	17
α-helix	90-93	4
β-strand	99-104	6	1
α-helix	110-120	11
α-helix	126-129	4
α-helix	133-137	5
α-helix	141-147	7
β-strand	156-157	2	1
β-strand	158-160	3	4
β-strand	161	1	5
β-strand	163	1	5
α-helix	165-178	14
β-strand	184-191	8	1
α-helix	195-203	9
β-strand	207	1	6
α-helix	215-217	3
β-strand	223	1	7
β-strand	229	1	6
β-strand	231-232	2	3
β-strand	234-242	9	1
α-helix	243-248	6
β-strand	255-264	10	1
α-helix	275-285	11
β-strand	294-296	3	1
α-helix	303-317	15
α-helix	321-322	2
β-strand	323-325	3	1
α-helix	328-331	4
β-strand	333	1	3
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	8
α-helix	356-357	2
β-strand	364	1	7
α-helix	366-368	3
β-strand	372-373	2	1
β-strand	378-379	2	8
β-strand	384-391	8	1
α-helix	392-394	3
β-strand	395-402	8	1

Chain B: 22 helices, 27 β-strands

Element	Residues	Length	Sheet
α-helix	1-3	3
β-strand	4-12	9	9
β-strand	13	1	10
β-strand	16	1	10
α-helix	19-28	10
β-strand	33-35	3	11
α-helix	37-42	6
β-strand	48-50	3	11
α-helix	62-65	4
α-helix	70-85	16
α-helix	90-93	4
β-strand	99-104	6	9
α-helix	110-121	12
α-helix	126-129	4
α-helix	133-137	5
α-helix	141-147	7
β-strand	156-157	2	9
β-strand	158-160	3	4
β-strand	161	1	12
β-strand	163	1	12
α-helix	165-178	14
β-strand	184-191	8	9
α-helix	195-202	8
β-strand	207	1	13
α-helix	215-218	4
β-strand	223	1	14
β-strand	229	1	13
α-helix	230	1
β-strand	231	1	15
β-strand	232	1	11
β-strand	234-242	9	9
α-helix	243-248	6
β-strand	255-264	10	9
α-helix	275-285	11
β-strand	294-296	3	9
α-helix	303-316	14
α-helix	321-322	2
β-strand	323-325	3	9
α-helix	328-331	4
β-strand	333	1	15
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	16
β-strand	364	1	14
α-helix	366-368	3
β-strand	373	1	9
β-strand	378-379	2	16
β-strand	384-391	8	9
β-strand	395-402	8	9

Chain C: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
β-strand	27	1	17
α-helix	36-50	15
α-helix	53-55	3
α-helix	56-61	6
β-strand	64	1	17
α-helix	65-73	9

Chain D: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13
α-helix	19-21	3
β-strand	27	1	18
α-helix	36-50	15
α-helix	56-61	6
β-strand	64	1	18
α-helix	65-75	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3-oxoacyl-[acyl-carrier-protein] synthase 1	A, B	protein	407	Escherichia coli	P0A953 (AlphaFold model)
Acyl carrier protein	C, D	protein	76	Escherichia coli	P0A6A8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9MLW_1 3-oxoacyl-[acyl-carrier-protein] synthase 1 (chains A, B)
VSKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGL
IDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGMGSPRFQVFGADA
MRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQL
GKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVV
VEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHG
TSTPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSI
NIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD

Sequence of entity 2 (C, D), FASTA

>9MLW_2 Acyl carrier protein (chains C, D)
TIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEK
ITTVQAAIDYINGHQA

Ligands and cofactors

ID	Name	Formula	Copies
A1BMZ	N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethy…	C19 H38 N3 O8 P	2

Primary citation

Biomolecular Plasticity Permits Diverse Product Profiles in Ketosynthase Mutants. Jiang, Z., Friedman, A.J., Thompson, A. et al. To be published.

Other PDB entries of the same protein (UniProt P0A953 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VBA 1.36 Å, beta-ketoacyl-ACP synthase I (KAS) from E. coli with bound amino- thiazole inhibitor
2VB9 1.5 Å, beta-ketoacyl-ACP synthase I (KAS) from E. coli, apo structure
2VB8 1.52 Å, beta-ketoacyl-ACP synthase I (KAS) from E. coli with bound inhibitor thiolactomycin
6OKC 1.55 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and…
2VB7 1.6 Å, beta-ketoacyl-ACP synthase I (KAS) from E. coli, apo structure after soak in PEG solution
2BYW 1.7 Å, Structure of Escherichia coli beta-ketoacyl (acyl carrier protein) synthase I LYS328ALA…
7SQI 1.7 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and…
1EK4 1.85 Å, Beta-ketoacyl [acyl carrier protein] synthase I in complex with dodecanoic acid to 1.85…
2BZ4 1.86 Å, structure of E.coli KAS I H298Q mutant
2BUH 1.9 Å, E. Coli beta-ketoacyl (acyl carrier protein) synthase I, 120 K
8SMS 1.93 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase, FabB, and cerulenin…
2BYZ 1.95 Å, Structure of E.coli KAS I H298Q mutant in complex with C12 fatty acid

Browse structure collections

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