5GXT: PigG

Crystal structure of PigG. Determined by X-ray diffraction at 2.25 Å resolution. Released 19 Jul 2017.

Method
X-ray diffraction
Resolution
2.25 Å
Organisms
Escherichia coli, Serratia sp. FS14
Chains
1
Atoms
3,593
Mol. weight
51.42 kDa
Ligands
MG
Released
19 Jul 2017

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

Secondary structure: helices and β-sheets

5GXT contains 25 α-helices and 23 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: 25 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand9-1241
α-helix19-3315
β-strand37-4041
α-helix45-539
β-strand61-6551
α-helix67-748
β-strand7812
α-helix79-813
α-helix85-884
β-strand9113
α-helix93-975
β-strand100-10124
β-strand104-10524
β-strand108-11361
β-strand116-12055
β-strand13016
α-helix131-1333
α-helix134-1429
β-strand147-14935
α-helix156-16510
β-strand171-17337
β-strand178-18367
α-helix188-20215
α-helix212-2209
β-strand224-22965
α-helix231-2333
α-helix234-2396
β-strand244-24745
α-helix248-2503
β-strand251-25226
β-strand255-25626
β-strand260-26128
β-strand262-26871
β-strand26912
α-helix275-2817
α-helix282-2865
α-helix289-29810
β-strand303-30421
β-strand30613
α-helix307-3137
α-helix317-32812
β-strand330-33128
α-helix332-3332
α-helix338-35316
α-helix359-38729
α-helix411-42313
α-helix429-4313
α-helix440-45415

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic protein,PigGAprotein468Escherichia coli, Serratia sp. FS14A0ACD6BAW2
Sequence of entity 1 (A), FASTA
>5GXT_1 Maltose-binding periplasmic protein,PigG (chains A)
MGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAHMLESKLIQHIATQYLDGDHDGLNAQTPLFELNVVDSASIFDLVDFLR
QESHVAIGMHEIHPANFASVQAMVALVQRLQAQVAAGGVALEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

Crystal structure of MBP-PigG fusion protein and the essential function of PigG in the prodigiosin biosynthetic pathway in Serratia marcescens FS14. Zhang, F., Wei, Q., Tong, H. et al. Int J Biol Macromol (2017) 99:394-400. DOI 10.1016/j.ijbiomac.2017.02.088 · PubMed

Other PDB entries of the same protein (UniProt A0ACD6BAW2), best resolution first:

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