2VB7: 3-oxoacyl-[acyl-carrier-protein] synthase 1

beta-ketoacyl-ACP synthase I (KAS) from E. coli, apo structure after soak in PEG solution. Determined by X-ray diffraction at 1.6 Å resolution. Released 25 Dec 2007.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: ESCHERICHIA COLI
Chains: 4
Atoms: 14,473
Mol. weight: 170.66 kDa
Released: 25 Dec 2007

Explore 2VB7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VB7 contains 87 α-helices and 100 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: 20 helices, 25 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	33-35	3	3
α-helix	37-41	5
β-strand	48-50	3	3
α-helix	62-65	4
α-helix	70-85	16
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
α-helix	162-164	3
α-helix	165-178	14
β-strand	184-191	8	1
α-helix	195-203	9
β-strand	207	1	5
α-helix	215-217	3
β-strand	223	1	6
β-strand	229	1	5
β-strand	231	1	7
β-strand	232	1	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	7
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	8
β-strand	364	1	6
β-strand	372-373	2	1
β-strand	378-379	2	8
β-strand	384-391	8	1
β-strand	395-402	8	1

Chain B: 22 helices, 25 β-strands

Element	Residues	Length	Sheet
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	37-41	5
β-strand	48-50	3	11
α-helix	62-65	4
α-helix	70-86	17
α-helix	90-93	4
β-strand	99-104	6	9
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	9
β-strand	158-160	3	4
α-helix	162-164	3
α-helix	165-178	14
β-strand	184-191	8	9
α-helix	195-203	9
β-strand	207	1	12
α-helix	215-217	3
β-strand	223	1	13
β-strand	229	1	12
β-strand	231	1	14
β-strand	232	1	11
β-strand	234-242	9	9
α-helix	243-248	6
α-helix	251-253	3
β-strand	255-264	10	9
α-helix	275-285	11
β-strand	294-296	3	9
α-helix	303-317	15
α-helix	321-322	2
β-strand	323-325	3	9
α-helix	328-331	4
β-strand	333	1	14
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	15
β-strand	364	1	13
α-helix	366-368	3
β-strand	373	1	9
β-strand	378-379	2	15
β-strand	384-391	8	9
β-strand	395-402	8	9

Chain C: 23 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	16
β-strand	13	1	17
β-strand	16	1	17
α-helix	19-28	10
β-strand	33-35	3	18
α-helix	37-41	5
β-strand	48-50	3	18
α-helix	62-65	4
α-helix	70-85	16
α-helix	90-93	4
β-strand	99-104	6	16
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	16
β-strand	158-160	3	19
α-helix	162-164	3
α-helix	165-178	14
β-strand	184-191	8	16
α-helix	195-203	9
β-strand	207	1	20
α-helix	215-217	3
β-strand	223	1	21
β-strand	229	1	20
β-strand	231	1	22
β-strand	232	1	18
β-strand	234-242	9	16
α-helix	243-248	6
β-strand	255-264	10	16
α-helix	275-285	11
α-helix	291-292	2
β-strand	294-296	3	16
α-helix	303-317	15
α-helix	321-322	2
β-strand	323-325	3	16
α-helix	328-331	4
β-strand	333	1	22
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	23
β-strand	364	1	21
α-helix	366-368	3
β-strand	373	1	16
β-strand	378-379	2	23
β-strand	384-391	8	16
β-strand	395-402	8	16
α-helix	403-405	3

Chain D: 22 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	24
β-strand	13	1	25
β-strand	16	1	25
α-helix	19-28	10
β-strand	33-35	3	26
α-helix	37-41	5
β-strand	48-50	3	26
α-helix	62-65	4
α-helix	70-86	17
α-helix	90-93	4
β-strand	99-104	6	24
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	24
β-strand	158-160	3	19
α-helix	162-164	3
α-helix	165-178	14
β-strand	184-191	8	24
α-helix	195-203	9
β-strand	207	1	27
α-helix	215-217	3
β-strand	223	1	28
β-strand	229	1	27
β-strand	231	1	29
β-strand	232	1	26
β-strand	234-242	9	24
α-helix	243-248	6
α-helix	251-253	3
β-strand	255-264	10	24
α-helix	275-285	11
β-strand	294-296	3	24
α-helix	303-317	15
α-helix	321-322	2
β-strand	323-325	3	24
α-helix	328-331	4
β-strand	333	1	29
α-helix	335-337	3
α-helix	338-352	15
β-strand	354-355	2	30
β-strand	364	1	28
α-helix	366-368	3
β-strand	372-373	2	24
β-strand	378-379	2	30
β-strand	384-391	8	24
β-strand	395-402	8	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3-oxoacyl-[acyl-carrier-protein] synthase 1	A, B, D	protein	406	ESCHERICHIA COLI	P0A953 (AlphaFold model)
3-oxoacyl-[acyl-carrier-protein] synthase 1	C	protein	406	ESCHERICHIA COLI	P0A953 (AlphaFold model)

Sequence of entity 1 (A, B, D), FASTA

>2VB7_1 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1 (chains A, B, D)
MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLI
DRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAM
RGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLG
KQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV
EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGT
STPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSIN
IEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD

Sequence of entity 2 (C), FASTA

>2VB7_2 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1 (chains C)
MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLI
DRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAM
RGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLG
KQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV
EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGT
STPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSIN
IEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD

Primary citation

Structure-Assisted Discovery of an Aminothiazole Derivative as a Lead Molecule for Inhibition of Bacterial Fatty-Acid Synthesis. Pappenberger, G., Schulz-Gasch, T., Kusznir, E. et al. Acta Crystallogr D Biol Crystallogr (2007) 63:1208. DOI 10.1107/S0907444907049852 · PubMed

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…
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
1H4F 2.0 Å, E. Coli beta-ketoacyl [acyl carrier protein] synthase I K328R

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