1CCZ: Protein

Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-a resolution. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Apr 1999.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,650
Mol. weight: 20.6 kDa
Ligands: NAG
Released: 5 Apr 1999

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

Secondary structure: helices and β-sheets

1CCZ contains 4 α-helices and 16 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: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	1
β-strand	13-15	3	2
α-helix	22-23	2
β-strand	26-30	5	1
β-strand	33-39	7	1
β-strand	42-45	4	1
α-helix	47-49	3
β-strand	53-55	3	2
β-strand	62-64	3	2
α-helix	69-71	3
β-strand	73-78	6	1
β-strand	86-93	8	1
α-helix	94-96	3
β-strand	100-104	5	3
β-strand	109-113	5	3
β-strand	121-126	6	4
β-strand	129-134	6	4
β-strand	138-142	5	3
β-strand	150-156	7	4
β-strand	159-165	7	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (CD58)	A	protein	171	Homo sapiens	P08921 (AlphaFold model), P19256 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CCZ_1 PROTEIN (CD58) (chains A)
FSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSG
SLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLEMVSKPMIYWECSNATLTCEVLEGTDV
ELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAVNRVSQESEMEVVNCPE

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution. Ikemizu, S., Sparks, L.M., van der Merwe, P.A. et al. Proc Natl Acad Sci U S A (1999) 96:4289-4294. DOI 10.1073/pnas.96.8.4289 · PubMed

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

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
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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