cd04981: IgV_H (this model, PSSM-Id:319286 is obsolete and has been replaced by 409370)
Immunoglobulin (Ig) heavy chain (H), variable (V) domain
IgV_H: Immunoglobulin (Ig) heavy chain (H), variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determine the type of immunoglobulin: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains.
Structure:1RHH_B; human monoclonal antibody X5 IgV light and heavy chain heterodimer interface, contacts based on 3.5 A distance. - View structure with Cn3D
Structure:1RHH_B; human monoclonal antibody X5 Fab light and heavy chain heterodimer interface (including constant domains of Fab), contacts based on 3.5 A distance. - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",