1MCP
PHOSPHOCHOLINE BINDING IMMUNOGLOBULIN FAB MC/PC603. AN X-RAY DIFFRACTION STUDY AT 2.7 ANGSTROMS
Summary for 1MCP
Entry DOI | 10.2210/pdb1mcp/pdb |
Descriptor | IGA-KAPPA MCPC603 FAB (LIGHT CHAIN), IGA-KAPPA MCPC603 FAB (HEAVY CHAIN), SULFATE ION, ... (4 entities in total) |
Functional Keywords | immunoglobulin |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 2 |
Total formula weight | 48528.91 |
Authors | Satow, Y.,Cohen, G.H.,Padlan, E.A.,Davies, D.R. (deposition date: 1984-07-09, release date: 1985-01-02, Last modification date: 2024-11-13) |
Primary citation | Satow, Y.,Cohen, G.H.,Padlan, E.A.,Davies, D.R. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. J.Mol.Biol., 190:593-604, 1986 Cited by PubMed Abstract: The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse myeloma protein, has been refined at 2.7 A resolution by a combination of restrained least-squares refinement and molecular modeling. The overall structure remains as previously reported, with an elbow bend angle between the variable and constant modules of 133 degrees. Some adjustments have been made in the structure of the loops as a result of the refinement. The hypervariable loops are all visible in the electron density map with the exception of three residues in the first hypervariable loop of the light chain. A sulfate ion occupies the site of binding of the phosphate moiety of phosphocholine. PubMed: 3097327DOI: 10.1016/0022-2836(86)90245-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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