1KAS: Beta-ketoacyl ACP synthase II

Beta-ketoacyl-ACP synthase II from escherichia coli. Determined by X-ray diffraction at 2.4 Å resolution. Released 2 Mar 1999.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,035
Mol. weight: 42.96 kDa
Released: 2 Mar 1999

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

Secondary structure: helices and β-sheets

1KAS contains 22 α-helices and 24 β-strands across 1 chain. 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, 24 β-strands

Element	Residues	Length	Sheet
β-strand	5-13	9	1
β-strand	14	1	2
β-strand	17	1	2
α-helix	20-28	9
β-strand	34-36	3	3
β-strand	49-51	3	3
α-helix	52-54	3
α-helix	64-67	4
α-helix	72-88	17
α-helix	97-99	3
β-strand	100-105	6	1
α-helix	111-124	14
α-helix	126-128	3
α-helix	133-137	5
α-helix	141-150	10
β-strand	156-157	2	1
α-helix	162-164	3
α-helix	165-179	15
β-strand	184-191	8	1
α-helix	196-204	9
β-strand	208	1	4
α-helix	215-218	4
β-strand	223	1	5
β-strand	229	1	4
β-strand	231	1	6
β-strand	232	1	3
β-strand	234-242	9	1
α-helix	243-249	7
β-strand	255-264	10	1
α-helix	271-273	3
α-helix	277-290	14
α-helix	294-296	3
β-strand	297-301	5	1
α-helix	308-322	15
β-strand	330-332	3	1
α-helix	335-338	4
β-strand	340	1	6
α-helix	342-344	3
α-helix	345-359	15
β-strand	361-362	2	7
β-strand	371	1	5
β-strand	378	1	1
α-helix	384	1
β-strand	385-386	2	7
β-strand	392-399	8	1
β-strand	403-410	8	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-ketoacyl ACP synthase II	A	protein	412	Escherichia coli	P0AAI5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KAS_1 BETA-KETOACYL ACP SYNTHASE II (chains A)
SKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCED
IISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTS
LMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYG
DADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVL
EEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYV
NAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQ
AVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI

Primary citation

Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. Huang, W., Jia, J., Edwards, P. et al. EMBO J (1998) 17:1183-1191. DOI 10.1093/emboj/17.5.1183 · PubMed

Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3HO9 1.9 Å, Structure of E.coli FabF(C163A) in complex with Platencin A1
3I8P 1.9 Å, Crystal structure of E. coli FabF(C163A) in complex with Platensimycin A1
3G11 2.0 Å, Structure of E. coli FabF(C163Q) in complex with dihydrophenyl platensimycin
3HO2 2.0 Å, Structure of E.coli FabF(C163A) in complex with Platencin
7L4E 2.0 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
2GFV 2.29 Å, Structure of E. coli FabF (KASII) C163Q mutant
6OKG 2.3 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
6OLT 2.35 Å, Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and…
2GFW 2.4 Å, Structure of wild type E. coli FabF (KASII)
2GFX 2.59 Å, Structure of E. coli FabF(C163Q) in complex with Platensimycin
3G0Y 2.6 Å, Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycin
1B3N 2.65 Å, Beta-ketoacyl carrier protein synthase as a drug target, implications from the crystal…

Browse structure collections

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