4ZYR: E. coli Lactose permease G46W/G262W

Crystal structure of E. coli Lactose permease G46W/G262W bound to p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG). Determined by X-ray diffraction at 3.31 Å resolution. Released 29 Jul 2015.

Method
X-ray diffraction
Resolution
3.31 Å
Organism
Escherichia coli (strain K12)
Chains
2
Atoms
6,241
Mol. weight
94.79 kDa
Ligands
9PG, BNG
Released
29 Jul 2015

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

Secondary structure: helices and β-sheets

4ZYR contains 59 α-helices and 0 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: 31 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix7-2620
α-helix30-323
α-helix33-375
α-helix45-528
α-helix60-6910
α-helix75-839
α-helix84-863
α-helix87-904
α-helix91-955
α-helix96-1016
α-helix108-1114
α-helix112-1143
α-helix115-1195
α-helix122-13211
α-helix141-16020
α-helix168-18619
α-helix210-2134
α-helix220-2289
α-helix229-2335
α-helix234-2396
α-helix243-2486
α-helix254-28633
α-helix288-30518
α-helix306-3083
α-helix312-34029
α-helix343-3453
α-helix346-3516
α-helix352-3565
α-helix357-3615
α-helix364-37613
α-helix378-39518
Chain B: 28 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix7-2418
α-helix30-356
α-helix45-528
α-helix56-6914
α-helix75-839
α-helix84-863
α-helix87-893
α-helix90-956
α-helix96-1005
α-helix105-1084
α-helix112-1143
α-helix115-1195
α-helix122-13211
α-helix140-16021
α-helix168-18619
α-helix210-2134
α-helix220-2289
α-helix229-2335
α-helix234-2396
α-helix243-2486
α-helix254-28633
α-helix288-30518
α-helix312-34029
α-helix343-3453
α-helix346-3516
α-helix352-3576
α-helix358-37316
α-helix378-39922

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lactose permeaseA, Bprotein417Escherichia coli (strain K12)P02920 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4ZYR_1 Lactose permease (chains A, B)
MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTWIIFAAISLFSLLFQ
PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA
GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALIL
AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD
QQFANFFTSFFATGEQGTRVFWYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS
VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL
AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA

Ligands and cofactors

IDNameFormulaCopies
9PG4-nitrophenyl alpha-D-galactopyranosideC12 H15 N O82
BNGnonyl beta-D-glucopyranosideC15 H30 O62

Primary citation

Structure of LacY with an alpha-substituted galactoside: Connecting the binding site to the protonation site. Kumar, H., Finer-Moore, J.S., Kaback, H.R. et al. Proc Natl Acad Sci U S A (2015) 112:9004-9009. DOI 10.1073/pnas.1509854112 · PubMed

Other PDB entries of the same protein (UniProt P02920 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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