6CSC: Citrate synthase

Chicken citrate synthase complex with trifluoroacetonyl-CoA and citrate. Determined by X-ray diffraction at 2.25 Å resolution. Released 24 Dec 1997.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Gallus gallus
Chains: 2
Atoms: 7,101
Mol. weight: 98.81 kDa
Ligands: CIT, COF
Released: 24 Dec 1997

Explore 6CSC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CSC contains 49 α-helices and 22 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: 25 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	6-28	23
β-strand	32-34	3	1
β-strand	37	1	2
α-helix	38-42	5
β-strand	49-52	4	3
β-strand	57-59	3	4
β-strand	63-65	3	4
β-strand	70	1	4
α-helix	71-77	7
β-strand	80	1	5
β-strand	87	1	5
α-helix	88	1
α-helix	89-98	10
α-helix	104-116	13
α-helix	122-128	7
α-helix	137-147	11
α-helix	148-151	4
α-helix	153-159	7
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	277-292	16
α-helix	298-310	13
α-helix	314-315	2
β-strand	318	1	6
α-helix	328-340	13
α-helix	345-364	20
β-strand	372	1	6
α-helix	374-376	3
α-helix	378-384	7
α-helix	390-392	3
α-helix	393-414	22
β-strand	423-425	3	7
α-helix	427-434	8

Chain B: 24 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	6-28	23
β-strand	32	1	2
β-strand	36-37	2	1
α-helix	38-42	5
β-strand	49-52	4	7
β-strand	56-59	4	8
β-strand	63-66	4	8
β-strand	69	1	8
α-helix	71-77	7
β-strand	80	1	9
β-strand	87	1	9
α-helix	88	1
α-helix	89-98	10
α-helix	104-117	14
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	243-253	11
α-helix	258-269	12
α-helix	277-292	16
α-helix	298-309	12
β-strand	318	1	10
α-helix	328-340	13
α-helix	345-363	19
β-strand	372	1	10
α-helix	375-384	10
α-helix	390-392	3
α-helix	393-414	22
β-strand	423-425	3	3
α-helix	427-434	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Citrate synthase	A, B	protein	437	Gallus gallus	P23007

Sequence of entity 1 (A, B), FASTA

>6CSC_1 CITRATE SYNTHASE (chains A, B)
ASSTNLKDVLASLIPKEQARIKTFRQQHGNTAVGQITVDMSYGGMRGMKGLIYETSVLDP
DEGIRFRGFSIPECQKLLPKAGGGEEPLPEGLFWLLVTGQIPTPEQVSWVSKEWAKRAAL
PSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGINRTKYWEFVYEDAMDLIA
KLPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEG
GNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLLWLSQLQKDLGADASDEK
LRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPSDPMFKLVAQLYKIVPNV
LLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLE
RPKSMSTAGLEKLSAGG

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	2
COF	Trifluoroacetonyl coenzyme a	C24 H37 F3 N7 O17 P3 S	2

Primary citation

Trifluoroacetonyl Coenzyme A, an Inhibitor of Citrate Synthase, Binds in a Combination of Productive and Nonproductive Modes. Usher, K.C., Branchaud, B., Remington, S.J. To be published.

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…
5CTS 1.9 Å, Proposed mechanism for the condensation reaction of citrate synthase. 1.9-Å structure of…
6CTS 2.5 Å, Proposed mechanism for the condensation reaction of citrate synthase. 1.9-Å structure of…

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