1PK0: EF3-CaM

Crystal Structure of the EF3-CaM complexed with PMEApp. Determined by X-ray diffraction at 3.3 Å resolution. Released 10 Feb 2004.

Method
X-ray diffraction
Resolution
3.3 Å
Organisms
Bacillus anthracis, Homo sapiens
Chains
6
Atoms
15,344
Mol. weight
227.15 kDa
Ligands
CA, EMA, YB
Released
10 Feb 2004

Explore 1PK0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PK0 contains 98 α-helices and 81 β-strands across 6 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: 26 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand296-29721
α-helix298-3058
α-helix309-32113
β-strand324-32851
α-helix333-3408
α-helix3431
β-strand344-34522
α-helix3461
α-helix352-3543
β-strand36312
β-strand36513
α-helix368-3703
α-helix377-39216
β-strand398-40253
β-strand40414
α-helix407-41610
β-strand420-42675
β-strand431-43665
β-strand442-44765
β-strand45214
β-strand453-45755
α-helix4581
β-strand472-47325
β-strand475-48173
β-strand484-48743
β-strand488-48922
β-strand494-49961
β-strand50016
α-helix501-5055
α-helix510-5178
α-helix523-53311
α-helix534-5385
β-strand541-54227
β-strand548-54927
α-helix551-56616
α-helix580-5823
β-strand594-59631
β-strand602-60431
α-helix608-61811
β-strand62416
α-helix648-6536
α-helix657-6593
α-helix660-6689
α-helix696-7049
α-helix707-7115
α-helix714-73623
α-helix743-76523
α-helix774-7774
α-helix789-7968
Chain B: 19 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand296-29728
α-helix299-3057
α-helix309-32113
β-strand324-32858
α-helix333-3408
β-strand344-34529
α-helix352-3543
β-strand36319
β-strand365110
α-helix368-3703
α-helix377-39216
β-strand398-402510
β-strand404111
α-helix407-4159
β-strand420-426712
β-strand431-436612
β-strand442-447612
β-strand452111
β-strand453-457512
α-helix4581
β-strand472-473212
β-strand475-481710
β-strand484-487410
β-strand488-48929
β-strand494-49968
β-strand500113
α-helix501-5077
α-helix510-5178
α-helix528-5336
α-helix534-5385
β-strand541114
β-strand549114
α-helix551-56515
α-helix580-5823
β-strand594-59638
β-strand602-60438
α-helix608-61811
β-strand624113
α-helix648-6514
α-helix714-72916
α-helix743-76523
α-helix786-79611
Chain C: 29 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand296-297215
α-helix298-3058
α-helix309-32113
β-strand324-328515
α-helix333-3408
α-helix3431
β-strand344-345216
α-helix3461
α-helix352-3543
β-strand363116
β-strand365117
α-helix368-3703
α-helix377-39216
β-strand398-402517
β-strand404118
α-helix407-41610
β-strand420-426719
β-strand431-436619
β-strand442-447619
β-strand452118
β-strand453-457519
α-helix4581
β-strand472-473219
β-strand475-481717
β-strand484-487417
β-strand488-489216
β-strand494-499615
β-strand500120
α-helix501-5055
α-helix514-5174
α-helix523-53311
α-helix534-5385
β-strand541-542221
β-strand548-549221
α-helix551-56616
α-helix580-5823
β-strand594-596315
β-strand602-604315
α-helix608-6158
α-helix616-6205
β-strand624120
α-helix648-6514
α-helix657-6593
α-helix661-6644
α-helix666-6694
α-helix670-6723
α-helix696-7049
α-helix707-7115
α-helix714-73825
α-helix743-76725
α-helix774-7774
α-helix789-7968
Chains D and E: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix6-1611
β-strand27122
α-helix29-3810
α-helix47-504
β-strand63122
α-helix65-7511
α-helix82-9211
β-strand99-100223
α-helix102-1109
α-helix118-12811
β-strand136-137223
α-helix138-1469
Chain F: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix6-1611
β-strand27126
α-helix29-3810
α-helix47-504
β-strand63126
α-helix65-7511
α-helix82-9211
β-strand99-100227
α-helix102-1109
α-helix118-12811
β-strand136-137227
α-helix138-1458

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Calmodulin-sensitive adenylate cyclaseA, B, Cprotein507Bacillus anthracisP40136 (AlphaFold model)
CalmodulinD, E, Fprotein147Homo sapiensP0DP23 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1PK0_1 Calmodulin-sensitive adenylate cyclase (chains A, B, C)
RIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVH
GKSSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIE
ELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFNW
RNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTN
LLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKDN
EIFIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITK
AKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHI
FSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSNI
EFKLLYKQLNFTENETDNFEVFQKIID
Sequence of entity 2 (D, E, F), FASTA
>1PK0_2 Calmodulin (chains D, E, F)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTA

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa6
EMA(adenin-9-yl-ethoxymethyl)-hydroxyphosphinyl-diphosphateC8 H14 N5 O10 P33
YBYtterbium (III) ionYb3

Primary citation

Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Shen, Y., Zhukovskaya, N.L., Zimmer, M.I. et al. Proc Natl Acad Sci U S A (2004) 101:3242-3247. DOI 10.1073/pnas.0306552101 · 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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