1NGZ
Chimeric Germline Fab 7g12-apo
Summary for 1NGZ
Entry DOI | 10.2210/pdb1ngz/pdb |
Related | 1N7M 1NGW 1NGX 1NGY 3FCT |
Descriptor | Germline Metal Chelatase Catalytic Antibody, Light chain, Germline Metal Chelatase Catalytic Antibody, Heavy chain (3 entities in total) |
Functional Keywords | antibody, immunoglobulin, antigen binding fragment (fab), immune system |
Biological source | Mus musculus, Homo sapiens (house mouse, human) More |
Total number of polymer chains | 2 |
Total formula weight | 46851.30 |
Authors | Yin, J.,Andryski, S.A.,Beuscher, A.B.,Stevens, R.C.,Schultz, P.G. (deposition date: 2002-12-18, release date: 2003-02-04, Last modification date: 2024-11-06) |
Primary citation | Yin, J.,Andryski, S.A.,Beuscher, A.B.,Stevens, R.C.,Schultz, P.G. Structural evidence for substrate strain in antibody catalysis Proc.Natl.Acad.Sci.USA, 100:856-861, 2003 Cited by PubMed Abstract: The crystal structure of the Michaelis complex between the Fab fragment of ferrochelatase antibody 7G12 and its substrate mesoporphyrin has been solved to 2.6-A resolution. The antibody-bound mesoporphyrin clearly adopts a nonplanar conformation and reveals that the antibody catalyzes the porphyrin metallation reaction by straining/distorting the bound substrate toward the transition-state configuration. The crystal structures of the Fab fragment of the germ-line precursor antibody to 7G12 and its complex with the hapten N-methylmesoporphyrin have also been solved. A comparison of these structures with the corresponding structures of the affinity-matured antibody 7G12 reveals the molecular mechanism by which the immune system evolves binding energy to catalyze this reaction. PubMed: 12552112DOI: 10.1073/pnas.0235873100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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