1HNG: Crystal structure

Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Determined by X-ray diffraction at 2.8 Å resolution. Released 7 Feb 1995.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Rattus rattus
Chains: 2
Atoms: 2,796
Mol. weight: 40.28 kDa
Released: 7 Feb 1995

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

Secondary structure: helices and β-sheets

1HNG contains 6 α-helices and 32 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, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
β-strand	14-16	3	2
α-helix	17-18	2
β-strand	27-34	8	1
β-strand	37-43	7	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
α-helix	99-101	3
β-strand	105-109	5	3
β-strand	114-118	5	3
β-strand	126-131	6	4
β-strand	134-139	6	4
β-strand	143-147	5	3
β-strand	155-161	7	4
β-strand	164-170	7	4

Chain B: 3 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	5
β-strand	14-16	3	6
β-strand	27-34	8	5
β-strand	37-43	7	5
α-helix	47-48	2
β-strand	49-50	2	5
β-strand	55-57	3	6
β-strand	63-65	3	6
α-helix	70-72	3
β-strand	74-82	9	5
β-strand	87-98	12	5
α-helix	99-101	3
β-strand	105-109	5	7
β-strand	114-118	5	7
β-strand	126-131	6	8
β-strand	134-139	6	8
β-strand	143-147	5	7
β-strand	155-161	7	8
β-strand	164-170	7	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CD2	A, B	protein	176	Rattus rattus	P08921 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1HNG_1 CD2 (chains A, B)
RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILAN
GDLKIKNLTRDDSGTYNVTVYSTNGTRILNKALDLRILEMVSKPMIYWECSNATLTCEVL
EGTDVELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAVNRVSQESEMEVVNCPE

Primary citation

Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Jones, E.Y., Davis, S.J., Williams, A.F. et al. Nature (1992) 360:232-239. DOI 10.1038/360232a0 · 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
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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