4BEP: Phosphocholine transferase ankx

Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein (apo-form). Determined by X-ray diffraction at 3.14 Å resolution. Released 24 Apr 2013.

Method
X-ray diffraction
Resolution
3.14 Å
Organism
LEGIONELLA PNEUMOPHILA
Chains
2
Atoms
7,531
Mol. weight
118.14 kDa
Ligands
MG
Released
24 Apr 2013

Explore 4BEP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BEP contains 67 α-helices and 18 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.

Chain A: 33 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix11-166
α-helix19-257
α-helix29-324
α-helix39-446
α-helix48-6114
α-helix74-818
β-strand106-11051
α-helix111-1133
β-strand11412
α-helix116-1249
α-helix126-1305
β-strand134-13741
β-strand138-14253
β-strand144-14743
α-helix160-17415
β-strand179-18461
α-helix190-20718
α-helix211-22818
α-helix235-2362
α-helix237-2437
α-helix245-2506
α-helix253-2564
β-strand26612
α-helix269-29123
α-helix294-2963
α-helix298-3003
α-helix305-31410
α-helix318-3247
α-helix335-34814
α-helix352-3598
α-helix363-3708
α-helix375-3784
α-helix380-3812
β-strand38214
β-strand39114
α-helix395-4028
α-helix405-4139
α-helix428-4358
α-helix438-44912
α-helix454-4585
α-helix468-4736
α-helix478-4792
Chain B: 34 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix11-166
α-helix19-257
α-helix29-324
α-helix39-446
α-helix48-6619
α-helix74-829
α-helix98-1003
β-strand106-11055
α-helix111-1133
β-strand11416
α-helix116-1249
α-helix126-1305
β-strand134-13745
α-helix157-1593
α-helix160-17415
β-strand179-18465
α-helix190-20718
α-helix211-22717
α-helix235-2362
α-helix237-2437
α-helix245-2506
α-helix253-2575
β-strand26616
α-helix269-29123
α-helix294-2963
α-helix305-31410
α-helix318-3247
α-helix333-34412
β-strand34817
β-strand35017
α-helix352-3598
α-helix363-3708
α-helix375-3784
β-strand38218
α-helix3831
α-helix388-3903
β-strand39118
α-helix395-4028
α-helix405-4139
α-helix428-4358
α-helix438-44912
α-helix454-4585
α-helix468-4747

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphocholine transferase ankxA, Bprotein512LEGIONELLA PNEUMOPHILAQ5ZXN6 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4BEP_1 PHOSPHOCHOLINE TRANSFERASE ANKX (chains A, B)
MSYYHHHHHHLESTSLYKKAGLENLYFQGVKIMPNLPGLYFLQAYPSEEIWRLFVDGRFW
SKENGWRGYESREPGCLNAALESLCSIALQVEKSGEEFELSVDLIKRIHKKCGKKVEELQ
EKNPGELRTDEPVSFGIPAGRASIKGIEEFLSLVFLTEGGAEFGPGKAGPFGPRFDKNYF
KNLNPEQIPDLAKQIYFDMCKYGHSNTNHFYLAVMKNVDVYLEKITQSYNKEIKTAETLD
EKLKIIVKHIRMYEVLHPFRDANGRTFVNNLLNIPLMQQGLPPATFYEPNVFDLYSAEEL
VVVVKEAIFNTVEIIEQSKRKTPITLYGYHSSLEEQTKFRDMLDSPSYEKIKHMDFSDLN
PEKLHLKTQKCLSSLNEQYPLHRGAIYLSDPGEIKLLLSNRNESQINQQIEQGAPPIYVG
KTPAHLAVISGNMAMLDELIAKKADLSLQDYDGKTALHYAAECGNMQIMGKILKVVLSQE
DAIKVLNIKDNHGKTAFHYAAEFGTPELISAL

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of the Legionella Effector Ankx Reveals the Mechanism of Phosphocholine Transfer by the Fic Domain. Campanacci, V., Mukherjee, S., Roy, C.R. et al. EMBO J (2013) 32:1469. DOI 10.1038/EMBOJ.2013.82 · PubMed

Other PDB entries of the same protein (UniProt Q5ZXN6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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