Summary for 7CAT
| Entry DOI | 10.2210/pdb7cat/pdb |
| Descriptor | CATALASE, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, h2o2 acceptor |
| Biological source | Bos taurus (bovine) |
| Cellular location | Peroxisome: P00432 |
| Total number of polymer chains | 2 |
| Total formula weight | 118052.75 |
| Authors | Murthy, M.R.N.,Reid III, T.J.,Sicignano, A.,Tanaka, N.,Fita, I.,Rossmann, M.G. (deposition date: 1984-11-15, release date: 1985-04-01, Last modification date: 2023-09-27) |
| Primary citation | Fita, I.,Rossmann, M.G. The NADPH binding site on beef liver catalase. Proc.Natl.Acad.Sci.USA, 82:1604-1608, 1985 Cited by PubMed Abstract: Beef liver and human erythrocyte catalases (EC 1.11.1.6) bind NADP tenaciously [Kirkman, H. N. & Gaetani, G. F. (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4348]. The position of NADP on beef liver catalase corresponds to the carboxyl-terminal polypeptide hinge in Penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain. In contrast to nearly all other known structures of protein-bound NADP, NAD, and FAD, the NADP molecule of beef liver catalase is folded into a right-handed helix and bound, in part, in the vicinity of the carboxyl end of two alpha-helices. A water molecule (W7) occupies a pseudosubstrate site close to the C4 position of the nicotinamide and is hydrogen bonded to His-304. Although the NADP and heme groups approach each other to within 13.7 A, there is no direct interaction. The function of the NADP remains a mystery. PubMed: 3856839DOI: 10.1073/pnas.82.6.1604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
