1CI5: Glycan-free mutant adhesion domain of human CD58

Glycan-free mutant adhesion domain of human CD58 (lfa-3). Determined by solution NMR. Released 22 Jun 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
776
Mol. weight
11 kDa
Released
22 Jun 1999

Explore 1CI5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CI5 contains 1 α-helix and 11 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, 11 β-strands

ElementResiduesLengthSheet
β-strand3-861
β-strand912
β-strand12-1543
β-strand26-3051
β-strand33-3971
β-strand42-4541
α-helix49-524
β-strand53-5533
β-strand62-6543
β-strand6712
β-strand74-7851
β-strand85-9391

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (lymphocyte function-associated antigen 3(CD58))Aprotein95Homo sapiensP19256 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1CI5_1 PROTEIN (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3(CD58)) (chains A)
SSQQIYGVKYGNVTFHVPSNQPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTKSG
SLTIYNLTSSDEDEYEMESPNITDSMKFFLYVGES

Primary citation

Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. Sun, Z.Y., Dotsch, V., Kim, M. et al. EMBO J (1999) 18:2941-2949. DOI 10.1093/emboj/18.11.2941 · PubMed

Other PDB entries of the same protein (UniProt P19256 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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