1CDC: CD2, N-terminal domain (1-99), truncated form

CD2, N-terminal domain (1-99), truncated form. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Sept 1995.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 1,628
Mol. weight: 22.32 kDa
Released: 15 Sept 1995

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

Secondary structure: helices and β-sheets

1CDC contains 6 α-helices and 20 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, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	3
β-strand	14-16	3	4
α-helix	17-18	2
β-strand	27-34	8	3
β-strand	37-43	7	3
α-helix	48-49	2
β-strand	50	1	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	86	1	3
β-strand	87-97	11	1

Chain B: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	1
β-strand	14-16	3	2
α-helix	17-18	2
β-strand	27-34	8	1
β-strand	37-43	7	1
α-helix	48-49	2
β-strand	50	1	3
β-strand	55-57	3	4
β-strand	63-65	3	4
α-helix	70-72	3
β-strand	74-82	9	3
β-strand	86	1	1
β-strand	87-98	12	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CD2	A, B	protein	99	Rattus norvegicus	P08921 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1CDC_1 CD2 (chains A, B)
RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILAN
GDLKIKNLTRDDSGTYNVTVYSTNGTRILDKALDLRILE

Primary citation

One sequence, two folds: a metastable structure of CD2. Murray, A.J., Lewis, S.J., Barclay, A.N. et al. Proc Natl Acad Sci U S A (1995) 92:7337-7341. DOI 10.1073/pnas.92.16.7337 · 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
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
1A7B 3.1 Å, Engineering a misfolded form of CD2
1T6W Rational design of a calcium-binding adhesion protein NMR, 20 structures

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