Structure of PDB 3vkq Chain A

Receptor sequence
>3vkqA (length=538) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
VAAERLEPRVEEKDGYWILKEQFRKGINPQEKVKIEKEPMKLFMENGIEE
LAKIPIEEIDQSKLTKDDIDVRLKWLGLFHRRKNQYGRFMMRLKLPNGVT
TSAQTRYLASVIRKYGKEGCADITTRQNWQIRGVVLPDVPEILKGLAEVG
LTSLQSGMDNVRNPVGNPLAGIDPEEIVDTRPYTNLLSQFITGNSRGNPA
VSNLPRKWNPCVVGSHDLYEHPHINDLAYMPATKDGRFGFNLLVGGFFSA
KRCDEAIPLDAWVPADDVVPVCRAILEAFRDLGFRGNRQKCRMMWLIDEL
GVEGFRAEVEKRMPQQQLERASPEDLVQKQWERRDYLGVHPQKQEGYSFI
GLHIPVGRVQADDMDELARLADEYGSGEIRLTVEQNIIIPNIETSKIEAL
LKEPVLSTFSPDPPILMKGLVACTGNQFCGQAIIETKARSLKITEEVQRQ
VSLTKPVRMHWTGCPNTCAQVQVADIGFMGCLTRDKNGKTVEGADVFLGG
RIGSDSHLGEVYKKAVPCDDLVPLVVDLLVNNFGAVPR
3D structure
PDB3vkq The reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet-visible microspectroscopy
ChainA
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) R109 R179 R223 K224 N226 C440 C446 G480 C481 C485 A486
Catalytic site (residue number reindexed from 1) R92 R162 R206 K207 N209 C423 C429 G463 C464 C468 A469
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:3vkq, PDBe:3vkq, PDBj:3vkq
PDBsum3vkq
PubMed22499059
UniProtQ76KB0

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