Structure of PDB 3b0h Chain B

Receptor sequence
>3b0hB (length=535) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
ERLEPRVEEKDGYWVLKEKFRQGINPAEKAKIEKEPMKLFMENGIEDLAK
ISLEEIEGSKLTKDDIDVRLKWLGLFHRRKHHYGRFMMRLKLPNGVTTSS
QTRYLASVIRKYGKDGCADVTTRQNWQIRGVVLPDVPEILKGLDEVGLTS
LQSGMDNVRNPVGNPLAGIDPHEIVDTRPYTNLLSQYVTANFRGNPAVTN
LPRKWNVCVIGSHDLYEHPQINDLAYMPATKDGRFGFNLLVGGFFSPKRC
AEAVPLDAWVPADDVVPVCKAILEAYRDLGTRGNRQKTRMMWLVDELGVE
GFRAEVVKRMPQQKLDRESTEDLVQKQWERREYLGVHPQKQEGYSFVGLH
IPVGRVQADDMDELARLADEYGSGELRLTVEQNIIIPNVKNSKIEALLNE
PLLKNRFSTDPPILMKNLVACTGNQFCGKAIIETKARSMKITEEVQLLVS
ITQPVRMHWTGCPNSCAQVQVADIGFMGCLTRKEGKTVEGADVYLGGRIG
SDSHLGDVYKKSVPCEDLVPIIVDLLVDNFGAVPR
3D structure
PDB3b0h Structure-function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high resolution structures
ChainB
Resolution2.306 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R109 R179 R223 K224 N226 C441 C447 G481 C482 C486 A487
Catalytic site (residue number reindexed from 1) R89 R159 R203 K204 N206 C421 C427 G461 C462 C466 A467
Enzyme Commision number 1.7.7.1: ferredoxin--nitrite reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0048307 ferredoxin-nitrite reductase activity
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0042128 nitrate assimilation

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Molecular Function
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Biological Process
External links
PDB RCSB:3b0h, PDBe:3b0h, PDBj:3b0h
PDBsum3b0h
PubMed22238192
UniProtQ76KA9

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