Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Beyond genetics: Deciphering the impact of missense variants in CAD deficiency.
Journal, issue, pages	J Inherit Metab Dis, Vol. 46, Page 1170-1185, Year 2023
Publish date	Jun 9, 2023 (structure data deposition date)
Authors	Del Cano-Ochoa, F. / Ng, B.G. / Rubio-Del-Campo, A. / Mahajan, S. / Wilson, M.P. / Vilar, M. / Rymen, D. / Sanchez-Pintos, P. / Kenny, J. / Ley Martos, M. ...Del Cano-Ochoa, F. / Ng, B.G. / Rubio-Del-Campo, A. / Mahajan, S. / Wilson, M.P. / Vilar, M. / Rymen, D. / Sanchez-Pintos, P. / Kenny, J. / Ley Martos, M. / Campos, T. / Wortmann, S.B. / Freeze, H.H. / Ramon-Maiques, S.
External links	J Inherit Metab Dis / PubMed:37540500
Methods	X-ray diffraction
Resolution	1.28 - 2.06 Å
Structure data	PDB-8pbe: Mutant K1556T of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate Method: X-RAY DIFFRACTION / Resolution: 1.71 Å PDB-8pbg: Mutant K1556T of the dihydroorotase domain of human CAD protein bound to the inhibitor fluoroorotate Method: X-RAY DIFFRACTION / Resolution: 1.46 Å PDB-8pbh: Mutant R1617Q of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate Method: X-RAY DIFFRACTION / Resolution: 1.87 Å PDB-8pbi: Mutant R1617Q of the dihydroorotase domain of human CAD protein bound to the inhibitor fluoroorotate Method: X-RAY DIFFRACTION / Resolution: 1.5 Å PDB-8pbj: Mutant R1722W of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate Method: X-RAY DIFFRACTION / Resolution: 1.55 Å PDB-8pbk: Mutant R1722W of the dihydroorotase domain of human CAD protein bound to the inhibitor fluoorotate Method: X-RAY DIFFRACTION / Resolution: 1.69 Å PDB-8pbm: Mutant R1789Q of the dihydroorotase domain of human CAD protein bound to the substrate dihydroorotate Method: X-RAY DIFFRACTION / Resolution: 1.28 Å PDB-8pbn: Mutant R1789Q of the dihydroorotase domain of human CAD protein bound to the inhibitor fluoorotate Method: X-RAY DIFFRACTION / Resolution: 1.71 Å PDB-8pbp: Mutant R1785C of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate Method: X-RAY DIFFRACTION / Resolution: 1.54 Å PDB-8pbq: Mutant R1810Q of the dihydroorotase domain of human CAD protein bound to the substrates Method: X-RAY DIFFRACTION / Resolution: 1.54 Å PDB-8pbr: Mutant R1475Q of the dihydroorotase domain of human CAD protein in apo form Method: X-RAY DIFFRACTION / Resolution: 2.06 Å PDB-8pbs: Mutant K1482M of the dihydroorotase domain of human CAD protein in apo form Method: X-RAY DIFFRACTION / Resolution: 2.05 Å PDB-8pbt: Mutant K1482M of the dihydroorotase domain of human CAD protein bound to the substrate dihydroorotate Method: X-RAY DIFFRACTION / Resolution: 1.43 Å PDB-8pbu: Mutant K1482M of the dihydroorotase domain of human CAD protein bound to the inhibitor fluoorotate Method: X-RAY DIFFRACTION / Resolution: 1.67 Å
Chemicals	ChemComp-FMT: FORMIC ACID ChemComp-NCD: N-CARBAMOYL-L-ASPARTATE ChemComp-ZN: Unknown entry ChemComp-HOH: WATER ChemComp-FOT: 5-FLUORO-2,6-DIOXO-1,2,3,6-TETRAHYDROPYRIMIDINE-4-CARBOXYLIC ACID ChemComp-NA: Unknown entry ChemComp-GOL: GLYCEROL ChemComp-DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
Source	homo sapiens (human)
Keywords	HYDROLASE / Nucleotide metabolism / de novo pyrimidine synthesis / CAD disease / multienzymatic protein / zinc / carboxylated lysine / BIOSYNTHETIC PROTEIN