1HN9: Beta-ketoacyl-ACP synthase III

Crystal structure of beta-ketoacyl-ACP synthase III. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Dec 2000.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Escherichia coli
Chains: 2
Atoms: 5,145
Mol. weight: 67.28 kDa
Ligands: PO4
Released: 27 Dec 2000

Explore 1HN9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HN9 contains 36 α-helices and 38 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: 18 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-11	10	1
β-strand	15-18	4	2
α-helix	19-23	5
α-helix	30-37	8
β-strand	41-44	4	2
α-helix	51-66	16
α-helix	70-72	3
β-strand	76-79	4	1
β-strand	85-87	3	3
α-helix	90-97	8
β-strand	102	1	4
β-strand	105-109	5	1
α-helix	111-113	3
α-helix	114-127	14
β-strand	133-140	8	1
α-helix	142-145	4
α-helix	151-154	4
β-strand	157	1	5
β-strand	160-169	10	1
β-strand	174-181	8	6
α-helix	183-188	6
β-strand	189-190	2	7
β-strand	191-192	2	8
α-helix	193-194	2
β-strand	206-207	2	7
α-helix	209-230	22
α-helix	235-237	3
β-strand	240-243	4	6
α-helix	248-257	10
α-helix	262-264	3
β-strand	265	1	6
α-helix	269-272	4
β-strand	274	1	5
α-helix	276-278	3
α-helix	279-289	11
β-strand	298-305	8	6
β-strand	309-316	8	6

Chain B: 18 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	1002-1011	10	1
β-strand	1015-1018	4	9
α-helix	1019-1023	5
α-helix	1030-1037	8
β-strand	1041-1044	4	9
α-helix	1051-1066	16
α-helix	1070-1072	3
β-strand	1075-1079	5	1
β-strand	1085-1087	3	8
α-helix	1090-1097	8
β-strand	1102	1	6
β-strand	1105-1109	5	1
α-helix	1111-1113	3
α-helix	1114-1127	14
β-strand	1133-1140	8	1
α-helix	1142-1145	4
α-helix	1151-1154	4
β-strand	1157	1	10
β-strand	1160-1169	10	1
β-strand	1174-1181	8	4
α-helix	1183-1188	6
β-strand	1189-1190	2	11
β-strand	1191-1192	2	3
α-helix	1193-1195	3
β-strand	1206-1207	2	11
α-helix	1209-1230	22
α-helix	1235-1237	3
β-strand	1240-1243	4	4
α-helix	1248-1258	11
α-helix	1262-1264	3
β-strand	1265	1	4
α-helix	1269-1272	4
β-strand	1274	1	10
α-helix	1276-1278	3
α-helix	1279-1289	11
β-strand	1298-1305	8	4
β-strand	1309-1316	8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-ketoacyl-acyl carrier protein synthase III	A, B	protein	317	Escherichia coli	P0A6R0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1HN9_1 BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (chains A, B)
MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAAT
RAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALS
VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLH
ADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDW
LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVL
LEAFGGGFTWGSALVRF

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

Primary citation

Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis. Qiu, X., Janson, C.A., Konstantinidis, A.K. et al. J Biol Chem (1999) 274:36465-36471. DOI 10.1074/jbc.274.51.36465 · PubMed

Other PDB entries of the same protein (UniProt P0A6R0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8D1U 1.3 Å, E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated…
6X7R 1.35 Å, E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with…
9KA5 1.42 Å, Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q from E. coli
1HNJ 1.46 Å, Crystal structure of beta-ketoacyl-ACP synthase III + malonyl-CoA
9KA6 1.47 Å, Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q in complex with acyl-ACP from…
9KA2 1.5 Å, Crystal structure of beta-ketoacyl-ACP synthase FabH from E. coli
1HND 1.6 Å, Crystal structure of beta-ketoacyl-ACP synthase III-CoA complex
5BNM 1.7 Å, E. coli FabH with Small Molecule Inhibitor 1
1EBL 1.8 Å, The 1.8 a crystal structure and active site architecture of beta-ketoacyl-[acyl carrier…
3IL9 1.85 Å, Structure of E. coli FabH
5BNR 1.89 Å, E. coli Fabh with small molecule inhibitor 2
1HNH 1.9 Å, Crystal structure of beta-ketoacyl-ACP synthase III + degraded form of acetyl-CoA

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