Editing Superoxide dismutase (section)

=== Human ===

There are three forms of superoxide dismutase present in humans, in all other [[mammals]], and most [[chordates]]. [[SOD1]] is located in the [[cytoplasm]], [[SOD2]] in the [[mitochondrion|mitochondria]], and [[SOD3]] is [[extracellular]]. The first is a [[protein dimer|dimer]] (consists of two units), whereas the others are tetramers (four subunits). SOD1 and SOD3 contain copper and zinc, whereas SOD2, the mitochondrial enzyme, has [[manganese]] in its reactive centre. The [[gene]]s are located on chromosomes 21, 6, and 4, respectively (21q22.1, 6q25.3 and 4p15.3-p15.1).
{|
|- valign=top
|{{infobox protein
| Name = [[SOD1|SOD1, soluble]]
| caption = Crystal structure of the human SOD1 enzyme (rainbow-color [[N-terminus]] = blue, [[C-terminus]] = red) complexed with copper (orange sphere) and zinc (grey sphere)<ref name="pmid">{{PDB|3CQQ}}; {{cite journal | vauthors = Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ | display-authors = 6 | title = Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis | journal = The Journal of Biological Chemistry | volume = 283 | issue = 23 | pages = 16169–16177 | date = June 2008 | pmid = 18378676 | pmc = 2414278 | doi = 10.1074/jbc.M801522200 | doi-access = free }}</ref>
| image = 2c9v CuZn rib n site.png
| width =
| HGNCid = 11179
| Symbol = [[SOD1]]
| AltSymbols = ALS, ALS1
| EntrezGene = 6647
| OMIM = 147450
| RefSeq = NM_000454
| UniProt = P00441
| PDB =
| ECnumber = 1.15.1.1
| Chromosome = 21
| Arm = q
| Band = 22.1
| LocusSupplementaryData =
}}
|{{infobox protein
| Name = [[SOD2|SOD2, mitochondrial]]
| caption = Active site of human mitochondrial Mn superoxide dismutase (SOD2)<ref name="pmid8605177">{{PDB|1VAR}}; {{cite journal | vauthors = Borgstahl GE, Parge HE, Hickey MJ, Johnson MJ, Boissinot M, Hallewell RA, Lepock JR, Cabelli DE, Tainer JA | display-authors = 6 | title = Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface | journal = Biochemistry | volume = 35 | issue = 14 | pages = 4287–4297 | date = April 1996 | pmid = 8605177 | doi = 10.1021/bi951892w | s2cid = 7450190 }}</ref>
| image = SODsite.gif
| width =
| HGNCid = 11180
| Symbol = [[SOD2]]
| AltSymbols = Mn-SOD; IPO-B; MVCD6
| EntrezGene = 6648
| OMIM = 147460
| RefSeq = NM_000636
| UniProt = P04179
| PDB =
| ECnumber = 1.15.1.1
| Chromosome = 6
| Arm = q
| Band = 25
| LocusSupplementaryData =
}}
|{{infobox protein
| Name = [[SOD3|SOD3, extracellular]]
| caption = Crystallographic structure of the tetrameric human SOD3 enzyme (cartoon diagram) complexed with copper and zinc cations (orange and grey spheres respectively)<ref name="pmid19289127">{{PDB|2JLP}}; {{cite journal | vauthors = Antonyuk SV, Strange RW, Marklund SL, Hasnain SS | title = The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding | journal = Journal of Molecular Biology | volume = 388 | issue = 2 | pages = 310–326 | date = May 2009 | pmid = 19289127 | doi = 10.1016/j.jmb.2009.03.026 }}</ref>
| image = SOD3_2JLP.png
| width =
| HGNCid = 11181
| Symbol = [[SOD3]]
| AltSymbols = EC-SOD; MGC20077
| EntrezGene = 6649
| OMIM = 185490
| RefSeq = NM_003102
| UniProt = P08294
| PDB =
| ECnumber = 1.15.1.1
| Chromosome = 4
| Arm = p
| Band = ter
| LocusSupplementaryData = -q21
}}
|}