1UXM

A4V mutant of human SOD1

Summary for 1UXM

Entry DOI	10.2210/pdb1uxm/pdb
Related	1AZV 1BA9 1DSW 1FUN 1HL4 1HL5 1KMG 1L3N 1MFM 1N18 1N19 1OEZ 1OZT 1OZU 1P1V 1PTZ 1PU0 1RK7 1SOS 1SPD 1UXL 4SOD
Descriptor	SUPEROXIDE DISMUTASE [CU-ZN], COPPER (II) ION, ZINC ION, ... (4 entities in total)
Functional Keywords	human cu, zn superoxide dismutase, antioxidant, metal- binding, amyotrophic lateral sclerosis, disease mutation, oxidoreductase
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cytoplasm: P00441
Total number of polymer chains	12
Total formula weight	191814.82
Authors	Hough, M.A.,Grossmann, J.G.,Antonyuk, S.V.,Strange, R.W.,Doucette, P.A.,Rodriguez, J.A.,Whitson, L.J.,Hart, P.J.,Hayward, L.J.,Valentine, J.S.,Hasnain, S.S. (deposition date: 2004-02-26, release date: 2004-03-19, Last modification date: 2023-12-13)
Primary citation	Hough, M.A.,Grossmann, J.G.,Antonyuk, S.V.,Strange, R.W.,Doucette, P.A.,Rodriguez, J.A.,Whitson, L.J.,Hart, P.J.,Hayward, L.J.,Valentine, J.S.,Hasnain, S.S. Dimer Destabilization in Superoxide Dismutase May Result in Disease-Causing Properties: Structures of Motor Neuron Disease Mutants Proc.Natl.Acad.Sci.USA, 101:5976-, 2004 Cited by PubMed: 15056757 DOI: 10.1073/PNAS.0305143101 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation