3CDC: Light Chain Amyloidogenic

kI O18/O8 N34I/Y87H immunoglobulin light chain variable domain. Determined by X-ray diffraction at 1.53 Å resolution. Released 2 Sept 2008.

Method
X-ray diffraction
Resolution
1.53 Å
Organism
Homo sapiens
Chains
2
Atoms
2,209
Mol. weight
23.89 kDa
Released
2 Sept 2008

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

Secondary structure: helices and β-sheets

3CDC contains 8 α-helices and 22 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: 4 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix1-33
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand33-3862
β-strand45-4952
β-strand53-5422
α-helix551
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand85-9062
α-helix961
β-strand97-9822
β-strand102-10652
Chain B: 4 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix0-23
β-strand4-743
β-strand10-1344
β-strand19-2573
β-strand33-3864
β-strand45-4954
β-strand53-5424
α-helix551
β-strand62-6653
β-strand70-7563
α-helix80-823
β-strand85-9064
α-helix961
β-strand97-9824
β-strand102-10654

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Light Chain AmyloidogenicA, Bprotein109Homo sapiensP01594 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3CDC_1 Light Chain Amyloidogenic (chains A, B)
STDIQMTQSPSSLSASVGDRVTITCQASQDISNYLIWYQQKPGKAPKLLIYDASNLETGV
PSRFSGSGSGTDFTFTISSLQPEDIATYHCQQYDNLPYTFGQGTKLEIK

Primary citation

Structural insights into the role of mutations in amyloidogenesis. Baden, E.M., Randles, E.G., Aboagye, A.K. et al. J Biol Chem (2008) 283:30950-30956. DOI 10.1074/jbc.M804822200 · PubMed

Other PDB entries of the same protein (UniProt P01594 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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