4ANP

Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone

Summary for 4ANP

Entry DOI	10.2210/pdb4anp/pdb
Related	1DMW 1J8T 1J8U 1KW0 1LRM 1MMK 1MMT 1PAH 1TDW 1TG2 2PAH 3PAH 4PAH 5PAH 6PAH
Descriptor	PHENYLALANINE-4-HYDROXYLASE, FE (III) ION, 5,6-DIMETHYL-3-(4-METHYL-2-PYRIDINYL)-2-THIOXO-2,3-DIHYDROTHIENO[2,3- D]PYRIMIDIN-4(1H)-ONE, ... (4 entities in total)
Functional Keywords	oxidoreductase, phenylketonuria, folding mechanism
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	1
Total formula weight	37903.77
Authors	Torreblanca, R.,Lira-Navarrete, E.,Sancho, J.,Hurtado-Guerrero, R. (deposition date: 2012-03-21, release date: 2012-04-11, Last modification date: 2023-12-20)
Primary citation	Torreblanca, R.,Lira-Navarrete, E.,Sancho, J.,Hurtado-Guerrero, R. Structural and Mechanistic Basis of the Interaction between a Pharmacological Chaperone and Human Phenylalanine Hydroxylase. Chembiochem, 13:1266-, 2012 Cited by PubMed Abstract: Not without a chaperone: Pharmacological chaperones are designed to bind and ideally stabilise their target protein. Here, we elucidate the molecular mechanism of a potential pharmacological chaperone to treat phenylketonuria. The crystal structure of human phenylalanine hydroxylase with compound IV may help in the rational design of more efficient compounds to treat this disease. PubMed: 22549968 DOI: 10.1002/CBIC.201200188 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.11 Å)

Structure validation