Structure of an open form of chicken heart citrate synthase at 2.8 Å resolution. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Apr 1991.
Explore 5CSC in 3D Show helices and sheets RCSB PDB PDBe
5CSC contains 55 α-helices and 17 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-26 | 20 | |
| β-strand | 32-37 | 6 | 1 |
| β-strand | 59 | 1 | 2 |
| β-strand | 63 | 1 | 2 |
| β-strand | 65 | 1 | 3 |
| β-strand | 70 | 1 | 3 |
| α-helix | 71-77 | 7 | |
| β-strand | 80 | 1 | 4 |
| β-strand | 87 | 1 | 4 |
| α-helix | 88 | 1 | |
| α-helix | 89-98 | 10 | |
| α-helix | 104-117 | 14 | |
| α-helix | 122-129 | 8 | |
| α-helix | 137-147 | 11 | |
| α-helix | 148-151 | 4 | |
| α-helix | 153-160 | 8 | |
| α-helix | 164-166 | 3 | |
| α-helix | 171-180 | 10 | |
| α-helix | 182-194 | 13 | |
| α-helix | 209-216 | 8 | |
| α-helix | 222-234 | 13 | |
| α-helix | 243-253 | 11 | |
| α-helix | 258-262 | 5 | |
| α-helix | 265-269 | 5 | |
| α-helix | 277-290 | 14 | |
| α-helix | 298-310 | 13 | |
| β-strand | 318 | 1 | 5 |
| α-helix | 328-339 | 12 | |
| α-helix | 345-363 | 19 | |
| β-strand | 372 | 1 | 5 |
| α-helix | 379-382 | 4 | |
| α-helix | 390-392 | 3 | |
| α-helix | 393-400 | 8 | |
| α-helix | 402-406 | 5 | |
| α-helix | 409-415 | 7 | |
| α-helix | 422-424 | 3 | |
| α-helix | 427-432 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-24 | 18 | |
| α-helix | 28-30 | 3 | |
| β-strand | 32-37 | 6 | 1 |
| α-helix | 38-41 | 4 | |
| β-strand | 57-59 | 3 | 6 |
| β-strand | 63-65 | 3 | 6 |
| β-strand | 70 | 1 | 6 |
| α-helix | 71-77 | 7 | |
| β-strand | 80 | 1 | 7 |
| β-strand | 87 | 1 | 7 |
| α-helix | 89-98 | 10 | |
| α-helix | 104-117 | 14 | |
| α-helix | 122-128 | 7 | |
| α-helix | 137-148 | 12 | |
| α-helix | 153-160 | 8 | |
| α-helix | 168-194 | 27 | |
| α-helix | 209-214 | 6 | |
| α-helix | 222-235 | 14 | |
| α-helix | 243-250 | 8 | |
| α-helix | 251-254 | 4 | |
| α-helix | 262-269 | 8 | |
| α-helix | 272-275 | 4 | |
| α-helix | 277-280 | 4 | |
| α-helix | 282-290 | 9 | |
| α-helix | 298-310 | 13 | |
| β-strand | 318 | 1 | 8 |
| α-helix | 328-337 | 10 | |
| α-helix | 345-363 | 19 | |
| β-strand | 372 | 1 | 8 |
| α-helix | 379-384 | 6 | |
| α-helix | 393-400 | 8 | |
| α-helix | 402-405 | 4 | |
| α-helix | 409-415 | 7 | |
| α-helix | 422-424 | 3 | |
| α-helix | 427-432 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Citrate synthase | A | protein | 433 | Gallus gallus | P23007 |
| Citrate synthase | B | protein | 429 | Gallus gallus | P23007 |
>5CSC_1 CITRATE SYNTHASE (chains A) ASSTNLKDVLAALIPKEQARIKTFRQQHGGTALGQITVDMSYGGMRGMKGLVYETSVLDP DEGIRFRGFSIPECQKLLPKGGXGGEPLPEGLFWLLVTGQIPTGAQVSWLSKEWAKRAAL PSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGILRTKYWEMVYESAMDLIA KLPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEG GNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLGWLAQLQKAXXXAGADAS LRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPGDPMFKLVAQLYKIVPNV LLEQGAAANPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLE RPKSMSTDGLIAL
>5CSC_2 CITRATE SYNTHASE (chains B) ASSTNLKDVLAALIPKEQARIKTFRQQHGGTALGQITVDMSYGGMRGMKGLVYETSVLDP DEGIRFRGFSIPECQKLLPKGGGGEPLPEGLFWLLVTGQIPTGAQVSWLSKEWAKRAALP SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGILRTKYWEMVYESAMDLIAK LPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGG NVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLGWLAQLQKAAGADASLRDY IWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPGDPMFKLVAQLYKIVPNVLLEQ GAAANPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKS MSTDGLIAL
Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution. Liao, D.-I., Karpusas, M., Remington, S.J. Biochemistry (1991) 30:6031-6036. DOI 10.1021/bi00238a029 · PubMed
Other PDB entries of the same protein (UniProt P23007), best resolution first:
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