Structure of PDB 1aoq Chain A

Receptor sequence
>1aoqA (length=551) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
HKTRTDNRYEPSLDNLAQQDVAAPGAPEGVTALSDAQYNEANKIYFERCA
GCHGVLRKGATGKALTPDLTRDLGFDYLQSFITYASPAGMPNWGTSGELS
AEQVDLMANYLLLDPAAPPEFGMKEMRESWKVHVAPEDRPTQQMNDWDLE
NLFSVTLRDAGQIALIDGSTYEIKTVLDTGYAVHISRLSASGRYLFVIGR
DGKVNMIDLWMKEPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPP
QYVIMDGETLEPKKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNV
KETGKILLVDYTDLNNLKTTEISAERFLHDGGLDGSHRYFITAANARNKL
VVIDTKEGKLVAIEDTGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVAL
IGTDPEGHPDNAWKILDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEI
SGSVAVFDIKAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTE
VWFSVWNGKDQESALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDT
Y
3D structure
PDB1aoq Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C65 C68 H69 M106 H345 H388
Catalytic site (residue number reindexed from 1) C49 C52 H53 M90 H329 H372
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:1aoq, PDBe:1aoq, PDBj:1aoq
PDBsum1aoq
PubMed9311786
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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