Structure of PDB 1as6 Chain C

Receptor sequence

>1as6C (length=335) Species: 511 (Alcaligenes faecalis)

TAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDD
AGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATG
ALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAI
MVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYE
DTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRP
HLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYV
NHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG

3D structure

• PDB: 1as6 Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications.
• Chain: C
• Resolution: 1.8 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): H91 D94 H96 H131 C132 H141 M146 H251 E275 T276 H302
• 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	NO2	C	H255 I257 H306	H251 I253 H302
BS02	CU	C	H95 C136 H145 M150	H91 C132 H141 M146
BS03	CU	C	H100 H135	H96 H131
BS04	NO2	C	D98 H100 H135	D94 H96 H131

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:1as6, PDBe:1as6, PDBj:1as6
• PDBsum: 1as6
• PubMed: 9353305
• UniProt: P38501|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)