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Structure of PDB 1snr Chain C

Receptor sequence >1snrC (length=336) Species: 511 (Alcaligenes faecalis) [Search protein sequence] ATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVID DAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAAT GALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGA IMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAY EDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTR PHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAY VNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG

3D structure PDB 1snr Side-on copper-nitrosyl coordination by nitrite reductase. Chain C Resolution 1.31 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) H95 D98 H100 H135 C136 H145 M150 H255 E279 T280 H306 Catalytic site (residue number reindexed from 1) H92 D95 H97 H132 C133 H142 M147 H252 E276 T277 H303 Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 NO C H255 I257 H306 H252 I254 H303 BS02 CU1 C H95 C136 H145 M150 H92 C133 H142 M147 BS03 CU C H100 H135 H97 H132 BS04 NO C D98 H100 H135 D95 H97 H132

Gene Ontology Molecular Function GO:0005507 copper ion binding GO:0016491 oxidoreductase activity GO:0046872 metal ion binding GO:0050421 nitrite reductase (NO-forming) activity

	Biological Process
GO:0019333	denitrification pathway
GO:0042128	nitrate assimilation

	Cellular Component
GO:0042597	periplasmic space

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