1UXL

I113T mutant of human SOD1

Summary for 1UXL

• Entry DOI: 10.2210/pdb1uxl/pdb
• Related: 1AZV 1BA9 1DSW 1FUN 1HL4 1HL5 1KMG 1L3N 1MFM 1N18 1N19 1OEZ 1OZT 1OZU 1P1V 1PTZ 1PU0 1RK7 1SOS 1SPD 1UXM 4SOD
• Descriptor: SUPEROXIDE DISMUTASE [CU-ZN], COPPER (II) ION, ZINC ION, ... (5 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: 10
• Total formula weight: 160213.13

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: 2004-02-25, 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; PubMed: 15056757; DOI: 10.1073/PNAS.0305143101

Experimental method

X-RAY DIFFRACTION (1.6 Å)