1A7B: Engineering a misfolded form of CD2

Engineering a misfolded form of CD2. Determined by X-ray diffraction at 3.1 Å resolution. Released 17 Jun 1998.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 2,956
Mol. weight: 43.59 kDa
Released: 17 Jun 1998

Explore 1A7B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A7B contains 6 α-helices and 36 β-strands across 4 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.

Chains A and C: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	1
β-strand	14-16	3	2
β-strand	27-34	8	1
β-strand	37-43	7	1
α-helix	48	1
β-strand	49-50	2	3
β-strand	57	1	4
β-strand	63-65	3	4
β-strand	74-82	9	3
β-strand	90-98	9	3

Chains B and D: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	3
β-strand	14-16	3	4
β-strand	27-34	8	3
β-strand	37-43	7	3
α-helix	48	1
β-strand	49-50	2	1
β-strand	55-57	3	2
β-strand	63-65	3	2
α-helix	70-72	3
β-strand	74-82	9	1
β-strand	87-98	12	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CD2	A, B, C, D	protein	97	Rattus norvegicus	P08921 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1A7B_1 CD2 (chains A, B, C, D)
RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKPFLKSGAFEILANGD
LKIKNLTRDDSGTYNVTVYSTNGTRILDKALDLRILE

Primary citation

Engineering an intertwined form of CD2 for stability and assembly. Murray, A.J., Head, J.G., Barker, J.J. et al. Nat Struct Biol (1998) 5:778-782. DOI 10.1038/1816 · PubMed

Other PDB entries of the same protein (UniProt P08921 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CCZ 1.8 Å, Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated…
1A64 2.0 Å, Engineering a misfolded form of rat CD2
1CDC 2.0 Å, CD2, N-terminal domain (1-99), truncated form
1A6P 2.08 Å, Engineering of a misfolded form of CD2
2DRU 2.6 Å, Crystal structure and binding properties of the CD2 and CD244 (2B4) binding protein, CD48
1HNG 2.8 Å, Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
1T6W Rational design of a calcium-binding adhesion protein NMR, 20 structures

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