Crystal structure of PigG. Determined by X-ray diffraction at 2.25 Å resolution. Released 19 Jul 2017.
Explore 5GXT in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 1 |
| α-helix | 19-33 | 15 | |
| β-strand | 37-40 | 4 | 1 |
| α-helix | 45-53 | 9 | |
| β-strand | 61-65 | 5 | 1 |
| α-helix | 67-74 | 8 | |
| β-strand | 78 | 1 | 2 |
| α-helix | 79-81 | 3 | |
| α-helix | 85-88 | 4 | |
| β-strand | 91 | 1 | 3 |
| α-helix | 93-97 | 5 | |
| β-strand | 100-101 | 2 | 4 |
| β-strand | 104-105 | 2 | 4 |
| β-strand | 108-113 | 6 | 1 |
| β-strand | 116-120 | 5 | 5 |
| β-strand | 130 | 1 | 6 |
| α-helix | 131-133 | 3 | |
| α-helix | 134-142 | 9 | |
| β-strand | 147-149 | 3 | 5 |
| α-helix | 156-165 | 10 | |
| β-strand | 171-173 | 3 | 7 |
| β-strand | 178-183 | 6 | 7 |
| α-helix | 188-202 | 15 | |
| α-helix | 212-220 | 9 | |
| β-strand | 224-229 | 6 | 5 |
| α-helix | 231-233 | 3 | |
| α-helix | 234-239 | 6 | |
| β-strand | 244-247 | 4 | 5 |
| α-helix | 248-250 | 3 | |
| β-strand | 251-252 | 2 | 6 |
| β-strand | 255-256 | 2 | 6 |
| β-strand | 260-261 | 2 | 8 |
| β-strand | 262-268 | 7 | 1 |
| β-strand | 269 | 1 | 2 |
| α-helix | 275-281 | 7 | |
| α-helix | 282-286 | 5 | |
| α-helix | 289-298 | 10 | |
| β-strand | 303-304 | 2 | 1 |
| β-strand | 306 | 1 | 3 |
| α-helix | 307-313 | 7 | |
| α-helix | 317-328 | 12 | |
| β-strand | 330-331 | 2 | 8 |
| α-helix | 332-333 | 2 | |
| α-helix | 338-353 | 16 | |
| α-helix | 359-387 | 29 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-431 | 3 | |
| α-helix | 440-454 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein,PigG | A | protein | 468 | Escherichia coli, Serratia sp. FS14 | A0ACD6BAW2 |
>5GXT_1 Maltose-binding periplasmic protein,PigG (chains A) MGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAHMLESKLIQHIATQYLDGDHDGLNAQTPLFELNVVDSASIFDLVDFLR QESHVAIGMHEIHPANFASVQAMVALVQRLQAQVAAGGVALEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
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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