2FD7: Chemically Synthesized Crambin

X-ray Crystal Structure of Chemically Synthesized Crambin. Determined by X-ray diffraction at 1.75 Å resolution. Released 16 Jan 2007.

Method
X-ray diffraction
Resolution
1.75 Å
Chains
1
Atoms
409
Mol. weight
4.74 kDa
Released
16 Jan 2007

Explore 2FD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FD7 contains 3 α-helices and 2 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: 3 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand2-321
α-helix7-1711
α-helix23-308
β-strand33-3421
α-helix42-443

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CrambinAprotein46P01542 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FD7_1 Crambin (chains A)
TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN

Primary citation

Role of a salt bridge in the model protein crambin explored by chemical protein synthesis: X-ray structure of a unique protein analogue, [V15A]crambin-alpha-carboxamide. Bang, D., Tereshko, V., Kossiakoff, A.A. et al. Mol Biosyst (2009) 5:750-756. DOI 10.1039/b903610e · PubMed

Other PDB entries of the same protein (UniProt P01542 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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