1F4N: Rop ALA2ILE2-6

C2 crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new fold. Determined by X-ray diffraction at 1.9 Å resolution. Released 10 Jan 2001.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Escherichia coli
Chains: 2
Atoms: 965
Mol. weight: 14.39 kDa
Ligands: CA
Released: 10 Jan 2001

Explore 1F4N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F4N 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

Element	Residues	Length	Sheet
α-helix	3-28	26
α-helix	32-54	23

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	8-28	21
α-helix	32-53	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rop ALA2ILE2-6	A, B	protein	63	Escherichia coli	P03051 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1F4N_1 ROP ALA2ILE2-6 (chains A, B)
GTKQEKTILNMARFIRSQALTILEKANELDADEIADIAESIHDHADEIYRSALARFGDDG
ENL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

Water and common crystallization additives (MPD) are not listed.

Primary citation

Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Willis, M.A., Bishop, B., Regan, L. et al. Structure (2000) 8:1319-1328. DOI 10.1016/S0969-2126(00)00544-X · PubMed

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

1NKD 1.09 Å, Atomic resolution (1.07 Å) structure of the rop mutant <2AA>
1RPO 1.4 Å, Restored heptad pattern continuity does not alter the folding of a 4-alpha-helical bundle
4DO2 1.4 Å, Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
2IJK 1.55 Å, Structure of a Rom protein dimer at 1.55 angstrom resolution
7KAE 1.6 Å, Rop protein variant with a buried tryptophan
1ROP 1.7 Å, Structure of the COL*E1 rop protein at 1.7 Å resolution
1B6Q 1.8 Å, Alanine 31 proline mutant of rop protein
2IJH 1.8 Å, Crystal structure analysis of ColE1 ROM mutant F14W
1GTO 1.82 Å, High resolution structure of a hyperstable helical bundle protein mutant
1GMG 1.9 Å, Alanine 31 proline mutant of rop protein, monoclinic form
2IJJ 1.9 Å, Crystal structure analysis of ColE1 ROM mutant F14Y
3K79 1.96 Å, C38A, C52V Cysteine-Free Variant of Rop (Rom)

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