Structure of PDB 1bl9 Chain A

Receptor sequence
>1bl9A (length=537) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQRCAGCHGVLRK
GATGKPLTPDITQQRGQQYLEALITYGTPLGMPNWGSSGELSKEQITLMA
KYIQHTPPQPPEWGMPEMRESWKVLVKPEDRPKKQLNDLDLPNLFSVTLR
DAGQIALVDGDSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMID
LWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYWPPQFAIMDGE
TLEPKQIVSTRGMTVDTQTYHPEPRVAAIIASHEHPEFIVNVKETGKVLL
VNYKDIDNLTVTSIGAAPFLHDGGWDSSHRYFMTAANNSNKVAVIDSKDR
RLSALVDVGKTPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHP
QYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDARISQSVAVFDL
KNLDAKYQVLPIAEWADLGEGAKRVVQPEYNKRGDEVWFSVWNGKNDSSA
LVVVDDKTLKLKAVVKDPRLITPTGKFNVYNTQHDVY
3D structure
PDB1bl9 Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C47 C50 H51 M88 H327 H369
Catalytic site (residue number reindexed from 1) C41 C44 H45 M82 H321 H363
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
1.7.99.1: hydroxylamine reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050418 hydroxylamine reductase activity
GO:0050421 nitrite reductase (NO-forming) activity
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:1bl9, PDBe:1bl9, PDBj:1bl9
PDBsum1bl9
PubMed9760233
UniProtP24474|NIRS_PSEAE Nitrite reductase (Gene Name=nirS)

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