2EZA: Phosphotransferase system, enzyme I

Amino terminal domain of enzyme I from escherichia coli, NMR, restrained regularized mean structure. Determined by solution NMR. Released 20 Aug 1997.

Method
Solution NMR
Organism
Escherichia coli
Chains
1
Atoms
1,989
Mol. weight
28.38 kDa
Released
20 Aug 1997

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

Secondary structure: helices and β-sheets

2EZA contains 12 α-helices and 9 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.

Chain A: 12 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand811
β-strand12-1871
α-helix22-243
α-helix33-6432
α-helix67-693
α-helix70-8011
α-helix83-9513
α-helix100-11617
α-helix121-14121
α-helix149-1513
β-strand156-16051
α-helix165-1706
β-strand176-18161
β-strand18212
α-helix189-1968
β-strand201-20221
β-strand20412
α-helix208-2103
β-strand217-22041
β-strand227-22931
α-helix233-25422

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphotransferase system, enzyme IAprotein259Escherichia coliP08839 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2EZA_1 PHOSPHOTRANSFERASE SYSTEM, ENZYME I (chains A)
MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK
AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD
EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI
TDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR
AVQEQVASEKAELAKLKDR

Primary citation

Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Tjandra, N., Garrett, D.S., Gronenborn, A.M. et al. Nat Struct Biol (1997) 4:443-449. DOI 10.1038/nsb0697-443 · PubMed

Other PDB entries of the same protein (UniProt P08839 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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