1CDB: CD2

Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. Determined by solution NMR. Released 31 Jan 1994.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 877
Mol. weight: 12.45 kDa
Released: 31 Jan 1994

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

Secondary structure: helices and β-sheets

1CDB contains 1 α-helix and 10 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: 1 helix, 10 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	6-10	5	1
β-strand	17	1	2
β-strand	32-36	5	1
β-strand	45-47	3	1
β-strand	54	1	1
β-strand	61	1	3
β-strand	69	1	3
β-strand	70	1	2
β-strand	80-86	7	1
β-strand	95-101	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CD2	A	protein	105	Homo sapiens	P06729 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CDB_1 CD2 (chains A)
KEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTY
KLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQER

Primary citation

Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. Withka, J.M., Wyss, D.F., Wagner, G. et al. Structure (1993) 1:69-81. DOI 10.1016/0969-2126(93)90009-6 · PubMed

Other PDB entries of the same protein (UniProt P06729 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2J6O 2.23 Å, Atypical polyproline recognition by the cms N-terminal SH3 domain. CMS:CD2 heterotrimer
1HNF 2.5 Å, Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at…
2J7I 2.9 Å, Atypical polyproline recognition by the cms N-terminal SH3 domain. CMS:CD2 heterodimer
1QA9 3.2 Å, Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3)…
1GYA N-glycan and polypeptide NMR solution structures of the adhesion domain of human CD2
1L2Z CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide

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