Structure of PDB 1nid Chain A

Receptor sequence

>1nidA (length=333) Species: 223 (Achromobacter cycloclastes)

DISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGT
EIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALG
GGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVL
PRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAV
KAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLI
GGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHN
LIEAFELGAAGHFKVTGEWNDDLMTSVVKPASM

3D structure

• PDB: 1nid The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted.
• Chain: A
• Resolution: 2.2 Å

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): H88 D91 H93 H128 C129 H138 M143 H248 E272 T273 H299
• 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	A	H95 C136 H145 M150	H88 C129 H138 M143
BS02	CU	A	H100 H135	H93 H128
BS03	NO2	A	D98 H135	D91 H128

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

External links

• PDB: RCSB:1nid, PDBe:1nid, PDBj:1nid
• PDBsum: 1nid
• PubMed: 7499203
• UniProt: P25006|NIR_ACHCY Copper-containing nitrite reductase (Gene Name=nirK)