1F4M: Rop ALA2ILE2-6
P3(2) crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new fold. Determined by X-ray diffraction at 2.25 Å resolution. Released 10 Jan 2001.
- Method
- X-ray diffraction
- Resolution
- 2.25 Å
- Organism
- Escherichia coli
- Chains
- 6
- Atoms
- 2,735
- Mol. weight
- 42.56 kDa
- Ligands
- CA
- Released
- 10 Jan 2001
Explore 1F4M in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1F4M contains 14 α-helices and 0 β-strands across 6 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 | 2-29 | 28 | |
| α-helix | 32-55 | 24 | |
Chain B: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 32-55 | 24 | |
Chain C: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 32-54 | 23 | |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-28 | 27 | |
| α-helix | 32-55 | 24 | |
Chain E: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6 | 1 | |
| α-helix | 7-11 | 5 | |
| α-helix | 12-28 | 17 | |
| α-helix | 32-56 | 25 | |
Chain F: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-28 | 24 | |
| α-helix | 32-55 | 24 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Rop ALA2ILE2-6 | A, B, C, D, E, F | protein | 63 | Escherichia coli | P03051 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>1F4M_1 ROP ALA2ILE2-6 (chains A, B, C, D, E, F)
GTKQEKTILNMARFIRSQALTILEKANELDADEIADIAESIHDHADEIYRSALARFGDDG
ENL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 6 |
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
- 1F4N 1.9 Å, C2 crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core…
- 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
Browse structure collections
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