1AMZ: Citrate synthase

Chicken citrate synthase complex with nitromethylde-CoA and malate. Determined by X-ray diffraction at 1.8 Å resolution. Released 24 Dec 1997.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Gallus gallus
Chains: 1
Atoms: 3,601
Mol. weight: 49.1 kDa
Ligands: MLT, NMX
Released: 24 Dec 1997

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

Secondary structure: helices and β-sheets

1AMZ contains 26 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: 26 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-28	23
α-helix	38-42	5
β-strand	56-59	4	1
β-strand	63-66	4	1
β-strand	69	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	104-117	14
α-helix	122-130	9
α-helix	137-147	11
α-helix	148-151	4
α-helix	153-159	7
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	277-288	12
α-helix	289-293	5
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	427-434	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Citrate synthase	A	protein	435	Gallus gallus	P23007

Sequence of entity 1 (A), FASTA

>1AMZ_1 CITRATE SYNTHASE (chains A)
STNLKDVLASLIPKEQARIKTFRQQHGNTAVGQITVDMSYGGMRGMKGLIYETSVLDPDE
GIRFRGFSIPECQKLLPKAGGGEEPLPEGLFWLLVTGQIPTPEQVSWVSKEWAKRAALPS
HVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGINRTKYWEFVYEDAMDLIAKL
PCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLLWLSQLQKDLGADASDEKLR
DYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPSDPMFKLVAQLYKIVPNVLL
EQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERP
KSMSTAGLEKLSAGG

Ligands and cofactors

ID	Name	Formula	Copies
MLT	D-malate	C4 H6 O5	1
NMX	Nitromethyldethia coenzyme a	C22 H37 N8 O18 P3	1

Primary citation

Mechanisms of Enzyme-Catalyzed Deprotonation of Acetyl-Coenzyme A. Schwartz, B., Vogel, K.W., Usher, K.C. et al. 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…
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…
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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