5CTS: Citrate synthase

Proposed mechanism for the condensation reaction of citrate synthase. 1.9-Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme a. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Oct 1990.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Gallus gallus
Chains: 1
Atoms: 3,468
Mol. weight: 48.28 kDa
Ligands: CMC, OAA
Released: 15 Oct 1990

Explore 5CTS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CTS contains 25 α-helices and 7 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: 25 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-28	23
α-helix	38-42	5
β-strand	57-59	3	1
β-strand	63-65	3	1
β-strand	70	1	1
α-helix	71-77	7
β-strand	80	1	2
β-strand	87	1	2
α-helix	88	1
α-helix	89-98	10
α-helix	101-103	3
α-helix	104-116	13
α-helix	122-130	9
α-helix	137-147	11
α-helix	148-151	4
α-helix	153-160	8
α-helix	164-166	3
α-helix	167-194	28
α-helix	209-217	9
α-helix	222-234	13
α-helix	243-252	10
α-helix	258-269	12
α-helix	277-288	12
α-helix	298-310	13
β-strand	318	1	3
α-helix	328-340	13
α-helix	345-364	20
β-strand	372	1	3
α-helix	375-384	10
α-helix	390-392	3
α-helix	393-414	22
α-helix	427-432	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Citrate synthase	A	protein	433	Gallus gallus	P23007

Sequence of entity 1 (A), FASTA

>5CTS_1 CITRATE SYNTHASE (chains A)
ASSTNLKDVLAALIPKEQARIKTFRQQHGGTALGQITVDMSYGGMRGMKGLVYETSVLDP
DEGIRFRGFSIPECQKLLPKGGXGGEPLPEGLFWLLVTGQIPTGAQVSWLSKEWAKRAAL
PSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGILRTKYWEMVYESAMDLIA
KLPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEG
GNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLGWLAQLQKAXXXAGADAS
LRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPGDPMFKLVAQLYKIVPNV
LLEQGAAANPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLE
RPKSMSTDGLIAL

Ligands and cofactors

ID	Name	Formula	Copies
CMC	Carboxymethyl coenzyme *a	C23 H38 N7 O18 P3 S	1
OAA	Oxaloacetate ion	C4 H3 O5	1

Primary citation

Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A. Karpusas, M., Branchaud, B., Remington, S.J. Biochemistry (1990) 29:2213-2219. DOI 10.1021/bi00461a002 · PubMed

Other PDB entries of the same protein (UniProt P23007), best resolution first:

1CSH 1.65 Å, A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor…
1CSC 1.7 Å, Structure of ternary complexes of citrate synthase with D-and L-malate: Mechanistic…
1CSI 1.7 Å, A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor…
1CSR 1.7 Å, Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-coa as inhibitors of of…
1CSS 1.7 Å, Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of of…
2CSC 1.7 Å, Structure of ternary complexes of CITRATE SYNTHASE WITH D-AND L-MALATE: mechanistic…
1AMZ 1.8 Å, Chicken citrate synthase complex with nitromethylde-CoA and malate
1AL6 1.85 Å, Chicken citrate synthase complex with N-hydroxyamido-CoA and oxaloacetate
3CSC 1.9 Å, Structure of ternary complexes of citrate synthase with D-and L-malate: mechanistic…
4CSC 1.9 Å, Structure of ternary complexes of citrate synthase with D-and L-malate: mechanistic…
6CSC 2.25 Å, Chicken citrate synthase complex with trifluoroacetonyl-CoA and citrate
6CTS 2.5 Å, Proposed mechanism for the condensation reaction of citrate synthase. 1.9-Å structure of…

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