Structure of PDB 1hj4 Chain B

Receptor sequence
>1hj4B (length=542) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
EPSLDNLAQQDVAAPGAPEGVSALSDAQYNEANKIYFERCAGCHGVLRKG
ATGKALTPDLTRDLGFDYLQSFITYGSPAGMPNWGTSGELSAEQVDLMAN
YLLLDPAAPPEFGMKEMRESWKVHVAPEDRPTQQENDWDLENLFSVTLRD
AGQIALIDGATYEIKSVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDL
WMKEPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGET
LEPKKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLV
DYTDLDNLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGK
LVAIEDTGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHP
DNAWKILDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDI
KAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGK
DQESALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY
3D structure
PDB1hj4 Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.
ChainB
Resolution1.6 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) C40 C43 H44 M81 H320 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:1hj4, PDBe:1hj4, PDBj:1hj4
PDBsum1hj4
PubMed11278884
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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