Structure of PDB 1gq1 Chain B

Receptor sequence
>1gq1B (length=559) Species: 82367 (Paracoccus pantotrophus) [Search protein sequence]
DPAAALEDHKTRTDNRSEPSLDNLAQQDVAAPGAPEGVSALSDAQYNEAN
KIYFERCAGCHGVLRKGATGKALTPDLTRDLGFDYLQSFITYGSPAGMPN
WGTSGELSAEQVDLMANYLLLDPAAPPEFGMKEMRESWKVHVAPEDRPTQ
QENDWDLENLFSVTLRDAGQIALIDGATYEIKSVLDTGYAVHISRLSASG
RYLFVIGRDGKVNMIDLWMKEPTTVAEIKIGSEARSIETSKMEGWEDKYA
IAGAYWPPQYVIMDGETLEPKKIQSTRGMTYDEQEYHPEPRVAAILASHY
RPEFIVNVKETGKILLVDYTDLDNLKTTEISAERFLHDGGLDGSHRYFIT
AANARNKLVVIDTKEGKLVAIEDTGGQTPHPGRGANFVHPTFGPVWATSH
MGDDSVALIGTDPEGHPDNAWKILDSFPALGGGSLFIKTHPNSQYLYVDA
TLNPEAEISGSVAVFDIKAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQG
EFNKDGTEVWFSVWNGKDQESALVVVDDKTLELKHVIKDERLVTPTGKFN
VYNTMTDTY
3D structure
PDB1gq1 Structure and Kinetic Properties of Paracoccus Pantotrophus Cytochrome Cd1 Nitrite Reductase with the D1 Heme Active Site Ligand Tyrosine 25 Replaced by Serine
ChainB
Resolution1.4 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) C57 C60 H61 M98 H337 H380
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:1gq1, PDBe:1gq1, PDBj:1gq1
PDBsum1gq1
PubMed12556530
UniProtP72181|NIRS_PARPN Nitrite reductase (Gene Name=nirS)

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