Structure of PDB 1rzq Chain C

Receptor sequence
>1rzqC (length=332) Species: 223 (Achromobacter cycloclastes) [Search protein sequence]
AAPVDISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVID
REGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAAT
GALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGA
IMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAY
EDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTR
PHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAY
VNHNLIEAFELGAAGHFKVTGEWNDDLMTSVV
3D structure
PDB1rzq pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes
ChainC
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 CU C H95 C136 H145 M150 H92 C133 H142 M147
BS02 CU C H100 H135 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rzq, PDBe:1rzq, PDBj:1rzq
PDBsum1rzq
PubMed15003518
UniProtP25006|NIR_ACHCY Copper-containing nitrite reductase (Gene Name=nirK)

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