5I4R: Contact-dependent inhibitor A

Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (trypsin-modified). Determined by X-ray diffraction at 3.3 Å resolution. Released 28 Jun 2017.

Method
X-ray diffraction
Resolution
3.3 Å
Organisms
Escherichia coli NC101, Escherichia coli
Chains
8
Atoms
8,941
Mol. weight
133.84 kDa
Ligands
GDP
Released
28 Jun 2017

Explore 5I4R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5I4R contains 40 α-helices and 74 β-strands across 8 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.

Chains A and E: 4 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand171-17221
α-helix1731
β-strand174-17522
β-strand179-18242
β-strand185-18842
α-helix189-1979
α-helix203-2119
β-strand216-21942
β-strand228-23252
β-strand235-24062
β-strand245-25172
α-helix252-2532
Chains B and F: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-4037
α-helix44-6623
α-helix74-829
α-helix88-9912
Chain C: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix10-112
β-strand12-1983
α-helix25-4016
Chain D: 11 helices, 28 β-strands
ElementResiduesLengthSheet
β-strand66-7163
β-strand76-8163
α-helix85-939
β-strand101-10773
β-strand11113
α-helix114-12613
β-strand131-13663
α-helix138-1403
α-helix144-16017
β-strand170-17233
α-helix175-1806
α-helix183-19917
α-helix201-2055
α-helix206-2083
β-strand212-21434
β-strand217-22151
β-strand225-23171
β-strand23414
β-strand236-23835
β-strand242-24764
β-strand249-25574
β-strand256-26161
β-strand265-26621
β-strand268-27035
β-strand274-28071
α-helix284-2863
β-strand28916
β-strand29116
β-strand292-29434
β-strand300-311127
α-helix312-3132
β-strand32318
β-strand330-33347
β-strand336-34387
α-helix344-3452
β-strand35118
β-strand356-369147
β-strand374-37967
β-strand382-392117
Chain G: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand12-19811
α-helix25-3915
Chain H: 10 helices, 28 β-strands
ElementResiduesLengthSheet
β-strand66-71611
β-strand76-81611
α-helix85-9410
β-strand101-107711
β-strand111111
α-helix114-12613
β-strand131-136611
α-helix144-16017
β-strand170-172311
α-helix175-1806
α-helix183-19917
α-helix201-2055
α-helix206-2083
β-strand212-214312
β-strand217-22159
β-strand225-23179
β-strand234112
β-strand236-238313
β-strand242-247612
β-strand249-255712
β-strand256-26169
β-strand265-26629
β-strand268-270313
β-strand274-27969
α-helix284-2863
β-strand289114
β-strand291114
β-strand292-294312
β-strand300-3111215
α-helix312-3132
β-strand323116
β-strand330-333415
β-strand336-343815
α-helix344-3452
β-strand351116
β-strand356-3691415
β-strand374-379615
β-strand382-3921115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Contact-dependent inhibitor AA, Eprotein92Escherichia coli NC101P0DSI1
Elongation factor TuC, Gprotein45Escherichia coliP0CE48 (AlphaFold model)
Elongation factor TuD, Hprotein335Escherichia coliP0CE47 (AlphaFold model)
Contact-dependent inhibitor IB, Fprotein114Escherichia coli NC101P0DSM8 (AlphaFold model)
Sequence of entity 1 (A, E), FASTA
>5I4R_1 Contact-dependent inhibitor A (chains A, E)
LSYLGIGKKISFDGDFYTVDGMKFSKSYYEKLWEQGRPAPFVQAREVLNSNPKIEPDPRG
APGYLRYEGAGLEMIYNPKTGQVGHIQPVKVK
Sequence of entity 2 (C, G), FASTA
>5I4R_2 Elongation factor Tu (chains C, G)
MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAAR
Sequence of entity 3 (D, H), FASTA
>5I4R_3 Elongation factor Tu (chains D, H)
GITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREH
ILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKAL
EGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV
GEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTI
KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKM
VVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
Sequence of entity 4 (B, F), FASTA
>5I4R_4 Contact-dependent inhibitor I (chains B, F)
MDIWPEFQRDLEMYRDVVLSIKRNLRLYEECIESLVHQIGSTNFDNAQPLFDDLFRMQSE
LATMLYKYEYKPGKRIQDLIYHLDRDDFYSRKYWHKKFSDGLAWPEAGHHHHHH

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22

Primary citation

Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs. Michalska, K., Gucinski, G.C., Garza-Sanchez, F. et al. Nucleic Acids Res (2017) 45:10306-10320. DOI 10.1093/nar/gkx700 · PubMed

Other PDB entries of the same protein (UniProt P0DSI1), best resolution first:

Browse structure collections

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