Structure of PDB 2akj Chain A

Receptor sequence
>2akjA (length=535) Species: 3562 (Spinacia oleracea) [Search protein sequence]
RLEPRVEERDGFWVLKEEFRSGINPAEKVKIEKDPMKLFIEDGISDLATL
SMEEVDKSKHNKDDIDVRLKWLGLFHRRKHHYGRFMMRLKLPNGVTTSEQ
TRYLASVIKKYGKDGCADVTTRQNWQIRGVVLPDVPEIIKGLESVGLTSL
QSGMDNVRNPVGNPLAGIDPHEIVDTRPFTNLISQFVTANSRGNLSITNL
PRKWNPCVIGSHDLYEHPHINDLAYMPATKNGKFGFNLLVGGFFSIKRCE
EAIPLDAWVSAEDVVPVCKAMLEAFRDLGFRGNRQKCRMMWLIDELGMEA
FRGEVEKRMPEQVLERASSEELVQKDWERREYLGVHPQKQQGLSFVGLHI
PVGRLQADEMEELARIADVYGSGELRLTVEQNIIIPNVENSKIDSLLNEP
LLKERYSPEPPILMKGLVACTGSQFCGQAIIETKARALKVTEEVQRLVSV
TRPVRMHWTGCPNSCGQVQVADIGFMGCMTRDENGKPCEGADVFVGGRIG
SDSHLGDIYKKAVPCKDLVPVVAEILINQFGAVPR
3D structure
PDB2akj Structure of Spinach Nitrite Reductase: Implications for Multi-electron Reactions by the Iron-Sulfur:Siroheme Cofactor
ChainA
Resolution2.8 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 L125 R179 R223 K224 N226 C441 C447 G481 C482 C486 G487
Catalytic site (residue number reindexed from 1) R88 L104 R158 R202 K203 N205 C420 C426 G460 C461 C465 G466
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
Cellular Component
GO:0009507 chloroplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2akj, PDBe:2akj, PDBj:2akj
PDBsum2akj
PubMed16331965
UniProtP05314|NIR_SPIOL Ferredoxin--nitrite reductase, chloroplastic (Gene Name=NIR)

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