Structure of PDB 1dy7 Chain B

Receptor sequence
>1dy7B (length=536) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
LAQQDVAAPGAPEGVSALSDAQYNEANKIYFERCAGCHGVLRKGATGKAL
TPDLTRDLGFDYLQSFITYGSPAGMPNWGTSGELSAEQVDLMANYLLLDP
AAPPEFGMKEMRESWKVHVAPEDRPTQQENDWDLENLFSVTLRDAGQIAL
IDGATYEIKSVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDLWMKEPT
TVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGETLEPKKI
QSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYTDLD
NLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVAIED
TGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNAWKI
LDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDIKAMTGD
GSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGKDQESAL
VVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY
3D structure
PDB1dy7 Proton-Coupled Structural Changes Upon Binding of Carbon Monoxide to Cytochrome Cd(1): A Combined Flash Photolysis and X-Ray Crystallography Study
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) C34 C37 H38 M75 H314 H357
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:1dy7, PDBe:1dy7, PDBj:1dy7
PDBsum1dy7
PubMed10998233
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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