Structure of PDB 1rzp Chain C Binding Site BS01

Receptor Information
>1rzp Chain C (length=332) Species: 223 (Achromobacter cycloclastes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAPVDISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVID
REGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAAT
GALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGA
IMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAY
EDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTR
PHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAY
VNHNLIEAFELGAAGHFKVTGEWNDDLMTSVV
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1rzp Chain C Residue 501 [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]
PDB1rzp pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes
Resolution1.9 Å
Binding residue
(original residue number in PDB)
H95 C136 H145 M150
Binding residue
(residue number reindexed from 1)
H92 C133 H142 M147
Annotation score1
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:1rzp, PDBe:1rzp, PDBj:1rzp
PDBsum1rzp
PubMed15003518
UniProtP25006|NIR_ACHCY Copper-containing nitrite reductase (Gene Name=nirK)

[Back to BioLiP]