Structure of PDB 1l9q Chain C Binding Site BS01

Receptor Information
>1l9q Chain C (length=336) Species: 511 (Alcaligenes faecalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVID
DAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAAT
GALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGA
IMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAY
EDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTR
PHLLGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAY
VNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG
Ligand information
Ligand IDNO2
InChIInChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1
InChIKeyIOVCWXUNBOPUCH-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		[O-]N=O
OpenEye OEToolkits 1.5.0N(=O)[O-]
FormulaN O2
NameNITRITE ION
ChEMBL
DrugBankDB12529
ZINC
PDB chain1l9q Chain A Residue 704 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1l9q Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine
Resolution1.7 Å
Binding residue
(original residue number in PDB)		D98 H100 H135
Binding residue
(residue number reindexed from 1)		D95 H97 H132
Annotation score5
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).
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1l9q, PDBe:1l9q, PDBj:1l9q
PDBsum1l9q
PubMed12538888
UniProtP38501|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)

[Back to BioLiP]