Structure of PDB 2avf Chain C

Receptor sequence
>2avfC (length=316) Species: 223 (Achromobacter cycloclastes) [Search protein sequence]
STLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEI
HAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGG
ALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPR
DGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAVKA
MRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGG
HGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLI
EAFELGAAGHFKVTGE
3D structure
PDB2avf Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes
ChainC
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H95 D98 H100 H135 C136 H145 M150 H255 E279 T280 H306
Catalytic site (residue number reindexed from 1) H86 D89 H91 H126 C127 H136 M141 H246 E270 T271 H297
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 H100 H135 H91 H126
BS02 CU C H95 C136 H145 M150 H86 C127 H136 M141
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:2avf, PDBe:2avf, PDBj:2avf
PDBsum2avf
PubMed16293231
UniProtP25006|NIR_ACHCY Copper-containing nitrite reductase (Gene Name=nirK)

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