Structure of PDB 1e2r Chain B

Receptor sequence
>1e2rB (length=543) Species: 266 (Paracoccus denitrificans) [Search protein sequence]
YEPSLDNLAQQDVAAPGAPEGVTALSDAQYNEANKIYFERCAGCHGVLRK
GATGKALTPDLTRDLGFDYLQSFITYASPAGMPNWGTSGELSAEQVDLMA
NYLLLDPAAPPEFGMKEMRESWKVHVAPEDRPTQQENDWDLENLFSVTLR
DAGQIALIDGSTYEIKTVLDTGYAVHISRLSASGRYLFVIGRDGKVNMID
LWMKEPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGE
TLEPKKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILL
VDYTDLNNLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEG
KLVAIEDTGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGH
PDNAWKILDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFD
IKAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNG
KDQESALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY
3D structure
PDB1e2r X-Ray Crystallographic Study of Cyanide Binding Provides Insights Into the Structure-Function Relationship for Cytochrome Cd1 Nitrite Reductase from Paracoccus Pantotrophus.
ChainB
Resolution1.59 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) C41 C44 H45 M82 H321 H364
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:1e2r, PDBe:1e2r, PDBj:1e2r
PDBsum1e2r
PubMed10827177
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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