Structure of PDB 1h9y Chain B

Receptor sequence
>1h9yB (length=519) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
LSDAQYNEANKIYFERCAGCHGVLRKGATGKALTPDLTRDLGFDYLQSFI
TYGSPAGMPNWGTSGELSAEQVDLMANYLLLDPAAPPEFGMKEMRESWKV
HVAPEDRPTQQENDWDLENLFSVTLRDAGQIALIDGATYEIKSVLDTGYA
VHISRLSASGRYLFVIGRDGKVNMIDLWMKEPTTVAEIKIGSEARSIETS
KMEGWEDKYAIAGAYWPPQYVIMDGETLEPKKIQSTRGMTYDEQEYHPEP
RVAAILASHYRPEFIVNVKETGKILLVDYTDLDNLKTTEISAERFLHDGG
LDGSHRYFITAANARNKLVVIDTKEGKLVAIEDTGGQTPHPGRGANFVHP
TFGPVWATSHMGDDSVALIGTDPEGHPDNAWKILDSFPALGGGSLFIKTH
PNSQYLYVDATLNPEAEISGSVAVFDIKAMTGDGSDPEFKTLPIAEWAGI
TEGQPRVVQGEFNKDGTEVWFSVWNGKDQESALVVVDDKTLELKHVIKDE
RLVTPTGKFNVYNTMTDTY
3D structure
PDB1h9y The Structure of an Alternative Form of Paracoccus Pantotrophus Cytochrome Cd1 Nitrite Reductase
ChainB
Resolution2.4 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) C17 C20 H21 M58 H297 H340
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:1h9y, PDBe:1h9y, PDBj:1h9y
PDBsum1h9y
PubMed11373294
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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