Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF). Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Jan 2002.
Explore 1K8T in 3D Show helices and sheets RCSB PDB PDBe
1K8T contains 25 α-helices and 27 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 | 296-297 | 2 | 1 |
| α-helix | 299-305 | 7 | |
| α-helix | 309-322 | 14 | |
| β-strand | 324-328 | 5 | 1 |
| α-helix | 329-331 | 3 | |
| α-helix | 336-340 | 5 | |
| α-helix | 343 | 1 | |
| β-strand | 344-345 | 2 | 2 |
| α-helix | 346 | 1 | |
| α-helix | 352-355 | 4 | |
| β-strand | 363 | 1 | 2 |
| β-strand | 365 | 1 | 3 |
| α-helix | 368-370 | 3 | |
| α-helix | 377-393 | 17 | |
| β-strand | 398-402 | 5 | 3 |
| β-strand | 404 | 1 | 4 |
| α-helix | 407-415 | 9 | |
| β-strand | 420 | 1 | 5 |
| β-strand | 424-427 | 4 | 6 |
| β-strand | 430-435 | 6 | 6 |
| β-strand | 436 | 1 | 5 |
| β-strand | 442-447 | 6 | 6 |
| β-strand | 452 | 1 | 4 |
| β-strand | 453-457 | 5 | 6 |
| β-strand | 472-473 | 2 | 6 |
| β-strand | 475-480 | 6 | 3 |
| β-strand | 485-487 | 3 | 3 |
| β-strand | 488-489 | 2 | 2 |
| β-strand | 494-499 | 6 | 1 |
| β-strand | 500 | 1 | 7 |
| α-helix | 501-507 | 7 | |
| α-helix | 510-516 | 7 | |
| α-helix | 527-535 | 9 | |
| α-helix | 551-565 | 15 | |
| β-strand | 593-596 | 4 | 1 |
| β-strand | 602-605 | 4 | 1 |
| α-helix | 608-614 | 7 | |
| α-helix | 615-619 | 5 | |
| α-helix | 620-622 | 3 | |
| β-strand | 624 | 1 | 7 |
| α-helix | 641-643 | 3 | |
| β-strand | 645-646 | 2 | 8 |
| β-strand | 653-654 | 2 | 8 |
| α-helix | 660-674 | 15 | |
| β-strand | 679 | 1 | 9 |
| α-helix | 687-706 | 20 | |
| α-helix | 707-710 | 4 | |
| α-helix | 714-737 | 24 | |
| β-strand | 741 | 1 | 9 |
| α-helix | 743-767 | 25 | |
| α-helix | 771-777 | 7 | |
| α-helix | 786-798 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin-sensitive adenylate cyclase | A | protein | 510 | Bacillus anthracis | P40136 (AlphaFold model) |
>1K8T_1 CALMODULIN-SENSITIVE ADENYLATE CYCLASE (chains A) DRIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNV HGKSSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRI EELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFN WRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVT NLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKD NEIFIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPIT KAKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANH IFSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSN IEFKLLYKQLNFTENETDNFEVFQKIIDEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
Water and common crystallization additives (SO4) are not listed.
Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Drum, C.L., Yan, S.-Z., Bard, J. et al. Nature (2002) 415:396-402. DOI 10.1038/415396a · PubMed
Other PDB entries of the same protein (UniProt P40136 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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