2CK2: Core-swapped mutant of fibronectin

Structure of core-swapped mutant of fibronectin. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Apr 2007.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,535
Mol. weight
20.43 kDa
Ligands
ACE
Released
10 Apr 2007

Explore 2CK2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CK2 contains 6 α-helices and 16 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: 3 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix51
β-strand6-1381
β-strand18-2361
β-strand31-3882
β-strand46-5162
β-strand56-5941
α-helix62-632
β-strand67-76102
β-strand83-8422
α-helix85-873
β-strand88-9362
Chain B: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand6-1382
β-strand17-2372
β-strand31-3881
α-helix44-452
β-strand46-5161
β-strand56-6052
α-helix62-632
β-strand67-7591
β-strand8411
α-helix85-873
β-strand88-9361

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Human fibronectinA, Bprotein96HOMO SAPIENSP02751 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2CK2_1 HUMAN FIBRONECTIN (chains A, B)
VSDVPRDIEVVAVTPTSALISWDAPAVTIRYIRLTYGETGGNSPVQEITLPGSKSTYTIS
GLKPGTDYTVTLYSVTGRGDSPASSKPASINFRTEI

Ligands and cofactors

IDNameFormulaCopies
ACEAcetyl groupC2 H4 O2

Primary citation

Designing an Extracellular Matrix Protein with Enhanced Mechanical Stability. Ng, S.P., Billings, K.S., Ohashi, T. et al. Proc Natl Acad Sci U S A (2007) 104:9633. DOI 10.1073/PNAS.0609901104 · PubMed

Other PDB entries of the same protein (UniProt P02751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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