1BL9AB

Conformational changes occurring upon reduction in nitrite reductase from pseudomonas aeruginosa
Link type Probability Chain A piercings Chain B piercings
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
view details
Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
view details
Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
view details
Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
view details
Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
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Hopf.2 Hopf.2 36% -115B -115A +268A -278A +318A -423A
Interpreting sequences
Chain A Sequence
AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMIDLWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGKTPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHPQYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRLITPTGKFNVYNTQHDVY
Chain A Sequence
AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMIDLWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGKTPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHPQYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRLITPTGKFNVYNTQHDVY
sequence length 537,537
structure length 537,537
publication title Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa.
pubmed doi rcsb
molecule tags Oxidoreductase
molecule keywords NITRITE REDUCTASE
ec nomenclature ec 1.7.2.1: Nitrite reductase (NO-forming).
ec 1.7.99.1: Hydroxylamine reductase.
ec 1.7.2.1: Nitrite reductase (NO-forming).
ec 1.7.99.1: Hydroxylamine reductase.
pdb deposition date1998-07-20
LinkProt deposition date2016-10-21

pfam database annotations

chain Pfam Accession CodePfam Family IdentifierPfam Description
AB PF02239 Cytochrom_D1Cytochrome D1 heme domain
AB PF13442 Cytochrome_CBB3Cytochrome C oxidase, cbb3-type, subunit III
AB PF02239 Cytochrom_D1Cytochrome D1 heme domain
AB PF13442 Cytochrome_CBB3Cytochrome C oxidase, cbb3-type, subunit III
Image from the rcsb pdb (www.rcsb.org)
cath code
ClassArchitectureTopologyHomologyDomain
1.10.760.10 Mainly Alpha Orthogonal Bundle Cytochrome Bc1 Complex; Chain D, domain 2 Cytochrome c 1bl9A01
2.140.10.20 Mainly Beta 8 Propellor Methanol Dehydrogenase; Chain A C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase 1bl9A02
1.10.760.10 Mainly Alpha Orthogonal Bundle Cytochrome Bc1 Complex; Chain D, domain 2 Cytochrome c 1bl9B01
2.140.10.20 Mainly Beta 8 Propellor Methanol Dehydrogenase; Chain A C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase 1bl9B02
1BL9AB 1NNOAB 1NIRAB
chains in the LinkProt database with same CATH superfamily
1BL9AB 1NNOAB 1NIRAB
chains in the LinkProt database with same CATH topology
1BL9AB 1NNOAB 1NIRAB
chains in the LinkProt database with same CATH homology


 
#chains in the LinkProt database with same CATH superfamily
 1BL9 AB;  1NNO AB;  1NIR AB; 
#chains in the LinkProt database with same CATH topology
 1BL9 AB;  1NNO AB;  1NIR AB; 
#chains in the LinkProt database with same CATH homology
 1BL9 AB;  1NNO AB;  1NIR AB; 
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#similar chains in the LinkProt database (?% sequence similarity)
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#similar chains, but unlinked
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#similar chains in the pdb database (?% sequence similarity)
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LinkProt | Interdisciplinary Laboratory of Biological Systems Modelling