3GLJ
A polymorph of carboxypeptidase B zymogen structure
Summary for 3GLJ
| Entry DOI | 10.2210/pdb3glj/pdb |
| Related | 1NSA |
| Descriptor | Carboxypeptidase B, ZINC ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | procarboxypeptidase b cpb zymogen metalloprotease polymorphic form, carboxypeptidase, disulfide bond, hydrolase, metal-binding, metalloprotease, protease, secreted, zymogen |
| Biological source | Sus scrofa (pig) |
| Cellular location | Secreted : P09955 |
| Total number of polymer chains | 1 |
| Total formula weight | 46410.95 |
| Authors | Fernandez, D. (deposition date: 2009-03-12, release date: 2009-10-20, Last modification date: 2024-10-16) |
| Primary citation | Fernandez, D.,Boix, E.,Pallares, I.,Aviles, F.X.,Vendrell, J. Analysis of a new crystal form of procarboxypeptidase B: further insights into the catalytic mechanism Biopolymers, 2009 Cited by PubMed Abstract: A new triclinic crystal structure form of porcine pancreatic procarboxypeptidase B (PCPB) was obtained at higher resolution than the previously known tetragonal crystal structure. This new crystal polymorph has allowed for a corrected, accurate assignment of residues along the polypeptide chain based on the currently available gene sequence information and crystallographic data. The present structure shows unbound PCPB in a distinct molecular packing as compared to the previous benzamidine complexed form. Its catalytically important Tyr248 residue is oriented and hydrogen-bonded to solvent water molecules, and locates the furthest away from the catalytic zinc ion as compared to previous structures. A relatively long stretch of residues flanking Tyr248 and guarding the access to the catalytic zinc ion was found to be sequentially unique to the M14 family of peptidases. Predictions from a normal mode analysis indicated that this stretch of residues belongs to a rigid subdomain in the protein structure. The specific presence of a tyrosyl residue at the most exposed position in this region would allow for a delicate balance between extreme hydrophobicity and hydrophilicity, and affect substrate binding and the kinetic efficiency of the enzyme. PubMed: 19802820DOI: 10.1002/bip.21320 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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