2IWY: Human mitochondrial beta-ketoacyl ACP synthase

Human mitochondrial beta-ketoacyl ACP synthase. Determined by X-ray diffraction at 2.06 Å resolution. Released 6 Feb 2007.

Method: X-ray diffraction
Resolution: 2.06 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 6,686
Mol. weight: 92.92 kDa
Released: 6 Feb 2007

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

Secondary structure: helices and β-sheets

2IWY contains 45 α-helices and 52 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: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	-1-40	4	1
β-strand	44-53	10	2
β-strand	56-57	2	2
α-helix	59-67	9
β-strand	73-75	3	3
α-helix	79-83	5
β-strand	88-90	3	3
α-helix	91-93	3
β-strand	94	1	4
β-strand	101	1	4
α-helix	103-105	3
α-helix	117-133	17
α-helix	140-144	5
β-strand	146-152	7	2
α-helix	157-170	14
α-helix	172-174	3
α-helix	179-183	5
α-helix	187-196	10
β-strand	202-203	2	2
β-strand	205	1	5
α-helix	208-210	3
α-helix	211-225	15
β-strand	230-237	8	2
α-helix	242-251	10
β-strand	254	1	6
β-strand	274	1	6
β-strand	276	1	7
β-strand	277	1	3
β-strand	279-287	9	2
α-helix	288-293	6
β-strand	300-309	10	2
α-helix	322-335	14
α-helix	339-341	3
β-strand	344-346	3	2
α-helix	353-367	15
α-helix	368-372	5
β-strand	375-377	3	2
α-helix	380-383	4
β-strand	385	1	7
α-helix	387-389	3
α-helix	390-404	15
β-strand	406-407	2	8
α-helix	408-409	2
β-strand	410	1	9
β-strand	426	1	9
β-strand	430-431	2	8
β-strand	439-446	8	2
β-strand	450-457	8	2

Chain B: 23 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	38-41	4	1
β-strand	44-53	10	10
β-strand	56-57	2	10
α-helix	59-67	9
β-strand	73-75	3	11
α-helix	79-81	3
β-strand	88-90	3	11
α-helix	91-93	3
β-strand	94	1	12
β-strand	101	1	12
α-helix	103-105	3
α-helix	109-112	4
α-helix	117-133	17
α-helix	140-144	5
β-strand	146-152	7	10
α-helix	157-170	14
α-helix	172-174	3
α-helix	179-183	5
α-helix	187-196	10
β-strand	202-203	2	10
β-strand	205	1	5
α-helix	208-210	3
α-helix	211-225	15
β-strand	230-237	8	10
α-helix	242-250	9
β-strand	254	1	13
β-strand	274	1	13
β-strand	276	1	14
β-strand	277	1	11
β-strand	279-287	9	10
α-helix	288-293	6
β-strand	300-309	10	10
α-helix	317-318	2
α-helix	322-335	14
α-helix	339-341	3
β-strand	344-346	3	10
α-helix	353-367	15
α-helix	368-372	5
β-strand	375-377	3	10
α-helix	380-383	4
β-strand	385	1	14
α-helix	387-389	3
α-helix	390-404	15
β-strand	406-407	2	15
β-strand	410	1	16
β-strand	426	1	16
β-strand	430-431	2	15
β-strand	439-446	8	10
β-strand	450-457	8	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3-oxoacyl-[acyl-carrier-protein] synthase	A, B	protein	438	HOMO SAPIENS	Q9NWU1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2IWY_1 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE (chains A, B)
MRGSHHHHHHGSIEGRSRLHRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEY
KSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTIMAIGAAELAMKDSGWHPQSEA
DQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP
NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPK
LACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEG
EGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKG
ATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEKRFIGL
TNSFGFGGTNATLCIAGL

Primary citation

Structure of the Human Beta-Ketoacyl [Acp] Synthase from the Mitochondrial Type II Fatty Acid Synthase. Christensen, C.E., Kragelund, B.B., von Wettstein-Knowles, P. et al. Protein Sci (2007) 16:261-272. DOI 10.1110/PS.062473707 · PubMed

Other PDB entries of the same protein (UniProt Q9NWU1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IWZ 1.65 Å, Human mitochondrial beta-ketoacyl ACP synthase complexed with hexanoic acid
2C9H 1.8 Å, Structure of mitochondrial beta-ketoacyl synthase
9N51 2.31 Å, Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and…
9N50 2.5 Å, Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and…

Browse structure collections

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