| Link type | Probability | Chain A piercings | Chain B piercings | Chain D piercings | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
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Hopf.1 U Ring | 44% | +51B +47D | +19A -34A +45A -143A | |||||||||
Chain A Sequence |
TIHKKGQAHWESDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS |
Chain A Sequence |
TIHKKGQAHWESDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS |
Chain A Sequence |
TIHKKGQAHWESDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS |
| sequence length | 142,142,142 |
| structure length | 142,142,142 |
| publication title |
Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC
pubmed doi rcsb |
| molecule tags | Hydroperoxide reductase |
| molecule keywords | osmotically inducible protein |
| source organism | Escherichia coli |
| ec nomenclature |
ec 1.11.1.15: Peroxiredoxin. ec 1.11.1.15: Peroxiredoxin. ec 1.11.1.15: Peroxiredoxin. |
| pdb deposition date | 2003-09-02 |
| LinkProt deposition date | 2016-10-22 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| ABD | PF02566 | OsmC | OsmC-like protein |
| ABD | PF02566 | OsmC | OsmC-like protein |
| ABD | PF02566 | OsmC | OsmC-like protein |
Image from the rcsb pdb (www.rcsb.org)cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 2-Layer Sandwich | GMP Synthetase; Chain A, domain 3 | GMP Synthetase; Chain A, domain 3 | ||
| Alpha Beta | 2-Layer Sandwich | GMP Synthetase; Chain A, domain 3 | GMP Synthetase; Chain A, domain 3 | ||
| Alpha Beta | 2-Layer Sandwich | GMP Synthetase; Chain A, domain 3 | GMP Synthetase; Chain A, domain 3 |
#chains in the LinkProt database with same CATH superfamily 1QWI CD; 1QWI BD; 1QWI AB; 1QWI ACD; 1QWI AC; 1QWI BCD; 1QWI ABC; 1QWI ABD; 1QWI BC; 1QWI ABCD; #chains in the LinkProt database with same CATH topology 1QWI ABC; 1FLO BD; 1FLO ABC; 1QWI BD; 1QWI CD; 1FLO AC; 1FLO ABCD; 1QWI ACD; 1FLO AD; 1QWI AC; 1FLO ABD; 1QWI BCD; 1FLO BC; 1QWI AB; 1QWI ABCD; 1QWI ABD; 1FLO BCD; 1QWI BC; 1FLO ACD; #chains in the LinkProt database with same CATH homology 1QWI CD; 1QWI BD; 1QWI AB; 1QWI ACD; 1QWI AC; 1QWI BCD; 1QWI ABC; 1QWI ABD; 1QWI BC; 1QWI ABCD;
#similar chains in the LinkProt database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unlinked ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...
