2VLQ: F86A mutant of E9 DNase domain

F86A mutant of E9 DNase domain in complex with Im9. Determined by X-ray diffraction at 1.6 Å resolution. Released 20 May 2008.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
ESCHERICHIA COLI
Chains
2
Atoms
2,048
Mol. weight
24.95 kDa
Ligands
MLA
Released
20 May 2008

Explore 2VLQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VLQ contains 20 α-helices and 13 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: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix7-93
α-helix12-2413
α-helix30-4415
α-helix51-544
α-helix56-572
α-helix64-7714
Chain B: 13 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix4-63
β-strand9-1021
β-strand1212
β-strand1613
α-helix22-276
β-strand32-3324
α-helix341
β-strand3513
α-helix36-427
β-strand46-4721
α-helix50-6314
α-helix65-684
α-helix73-808
α-helix83-853
β-strand8615
α-helix87-882
α-helix89-913
β-strand9316
β-strand9616
β-strand9815
β-strand100-10344
α-helix107-1093
β-strand11512
α-helix116-1183
β-strand119-12244
α-helix124-13310

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Colicin-E9 immunity proteinAprotein86ESCHERICHIA COLIP13479 (AlphaFold model)
Colicin E9Bprotein134ESCHERICHIA COLIP09883 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2VLQ_1 COLICIN-E9 IMMUNITY PROTEIN (chains A)
MELKHSISDYTEAEFLQLVTTICNADTSSEEELVKLVTHFEEMTEHPSGSDLIYYPKEGD
DDSPSGIVNTVKQWRAANGKSGFKQG
Sequence of entity 2 (B), FASTA
>2VLQ_2 COLICIN E9 (chains B)
MESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEE
VSKDPELSKNLNPSNKSSVSKGYSPATPKNQQVGGRKVYELHHDKPISQGGEVYDMDNIR
VTTPKRHIDIHRGK

Ligands and cofactors

IDNameFormulaCopies
MLAMalonic acidC3 H4 O43

Primary citation

Experimental and Computational Analyses of the Energetic Basis for Dual Recognition of Immunity Proteins by Colicin Endonucleases. Keeble, A.H., Joachimiak, L.A., Mate, M.J. et al. J Mol Biol (2008) 379:745. DOI 10.1016/J.JMB.2008.03.055 · PubMed

Other PDB entries of the same protein (UniProt P13479 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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