1GMG: Regulatory protein rop

Alanine 31 proline mutant of rop protein, monoclinic form. Determined by X-ray diffraction at 1.9 Å resolution. Released 12 Sept 2002.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
ESCHERICHIA COLI
Chains
2
Atoms
943
Mol. weight
14.53 kDa
Released
12 Sept 2002

Explore 1GMG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GMG contains 4 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-2624
α-helix31-5424
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-2623
α-helix31-5424

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulatory protein ropA, Bprotein63ESCHERICHIA COLIP03051 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1GMG_1 REGULATORY PROTEIN ROP (chains A, B)
MTKQEKTALNMARFIRSQTLTLLEKLNELDPDEQADICESLHDHADELYRSCLARFGDDG
ENL

Primary citation

Structure Determination of a Small Protein Through a 23-Dimensional Molecular-Replacement Search. Glykos, N.M., Kokkinidis, M. Acta Crystallogr D Biol Crystallogr (2003) 59:709. DOI 10.1107/S0907444903002889 · PubMed

Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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