Structure of activated aconitase. Formation of the (4FE-4S) cluster in the crystal. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Jul 1990.
Explore 6ACN in 3D Show helices and sheets RCSB PDB PDBe
6ACN contains 39 α-helices and 52 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 1 |
| β-strand | 15 | 1 | 1 |
| α-helix | 18-32 | 15 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-44 | 7 | |
| β-strand | 47 | 1 | 2 |
| β-strand | 61-64 | 4 | 2 |
| β-strand | 68-72 | 5 | 3 |
| α-helix | 73-86 | 14 | |
| β-strand | 95-98 | 4 | 3 |
| β-strand | 105 | 1 | 4 |
| α-helix | 109-134 | 26 | |
| β-strand | 137-139 | 3 | 3 |
| α-helix | 140 | 1 | |
| β-strand | 144 | 1 | 5 |
| α-helix | 146-149 | 4 | |
| α-helix | 150-154 | 5 | |
| β-strand | 160-163 | 4 | 3 |
| α-helix | 168-174 | 7 | |
| β-strand | 177-180 | 4 | 3 |
| α-helix | 183-191 | 9 | |
| α-helix | 193-194 | 2 | |
| β-strand | 195-198 | 4 | 2 |
| α-helix | 199-200 | 2 | |
| β-strand | 201-208 | 8 | 6 |
| α-helix | 217-232 | 16 | |
| β-strand | 236-241 | 6 | 6 |
| α-helix | 243-247 | 5 | |
| α-helix | 250-259 | 10 | |
| α-helix | 260-263 | 4 | |
| β-strand | 267-269 | 3 | 6 |
| α-helix | 274-282 | 9 | |
| α-helix | 286-293 | 8 | |
| α-helix | 296-298 | 3 | |
| α-helix | 301-302 | 2 | |
| β-strand | 309-314 | 6 | 6 |
| β-strand | 321 | 1 | 7 |
| β-strand | 323 | 1 | 8 |
| β-strand | 333 | 1 | 7 |
| α-helix | 334-344 | 11 | |
| β-strand | 349 | 1 | 9 |
| β-strand | 350-356 | 7 | 8 |
| β-strand | 360 | 1 | 8 |
| α-helix | 363-377 | 15 | |
| β-strand | 386-390 | 5 | 8 |
| β-strand | 393 | 1 | 5 |
| α-helix | 394-402 | 9 | |
| α-helix | 405-411 | 7 | |
| β-strand | 414-416 | 3 | 8 |
| α-helix | 422-424 | 3 | |
| β-strand | 428 | 1 | 4 |
| β-strand | 439-443 | 5 | 8 |
| β-strand | 459-463 | 5 | 8 |
| α-helix | 466-475 | 10 | |
| β-strand | 477 | 1 | 9 |
| β-strand | 487-488 | 2 | 10 |
| β-strand | 494-495 | 2 | 10 |
| α-helix | 497-500 | 4 | |
| β-strand | 517-518 | 2 | 3 |
| β-strand | 538 | 1 | 11 |
| α-helix | 543-547 | 5 | |
| β-strand | 552-560 | 9 | 12 |
| β-strand | 561 | 1 | 13 |
| β-strand | 566 | 1 | 14 |
| α-helix | 567-570 | 4 | |
| β-strand | 571 | 1 | 15 |
| α-helix | 574-579 | 6 | |
| β-strand | 581 | 1 | 11 |
| α-helix | 583-586 | 4 | |
| α-helix | 587-589 | 3 | |
| β-strand | 590 | 1 | 15 |
| β-strand | 595-596 | 2 | 13 |
| β-strand | 601-602 | 2 | 13 |
| β-strand | 605-606 | 2 | 16 |
| β-strand | 613-614 | 2 | 16 |
| α-helix | 616-624 | 9 | |
| β-strand | 630-633 | 4 | 12 |
| β-strand | 638 | 1 | 17 |
| β-strand | 640 | 1 | 14 |
| α-helix | 646-653 | 8 | |
| β-strand | 656-661 | 6 | 12 |
| β-strand | 664 | 1 | 17 |
| α-helix | 666-674 | 9 | |
| β-strand | 678-682 | 5 | 12 |
| α-helix | 685-689 | 5 | |
| β-strand | 696-700 | 5 | 12 |
| α-helix | 702-704 | 3 | |
| β-strand | 711-716 | 6 | 12 |
| β-strand | 722-728 | 7 | 12 |
| α-helix | 733-741 | 9 | |
| α-helix | 744-750 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aconitase | A | protein | 754 | Sus scrofa | P16276 (AlphaFold model) |
>6ACN_1 ACONITASE (chains A) QRAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKT YLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDIN QEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIG VGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEY HGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLV PDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTN SSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANA CGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKF NPETDFLTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDSSGQRVDVSPTSQRLQL LEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENR KANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRHLGGRAII TKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPGKPLKCIIKHPNG TQETILLNHTFNETQIEWFRAGSALNRMKELQQK
Water and common crystallization additives (SO4) are not listed.
Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Robbins, A.H., Stout, C.D. Proc Natl Acad Sci U S A (1989) 86:3639-3643. DOI 10.1073/pnas.86.10.3639 · PubMed
Other PDB entries of the same protein (UniProt P16276 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6ACN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.