Structure of PDB 2pp8 Chain A Binding Site BS03
Receptor Information
>2pp8 Chain A (length=336) Species:
511
(Alcaligenes faecalis) [
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ATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVID
DAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAAT
GALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGA
IMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAY
EDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTR
PHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAY
VNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG
Ligand information
Ligand ID
ACT
InChI
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKey
QTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
[O-]C(=O)C
OpenEye OEToolkits 1.5.0
CC(=O)[O-]
CACTVS 3.341
CC([O-])=O
Formula
C2 H3 O2
Name
ACETATE ION
ChEMBL
DrugBank
DB14511
ZINC
PDB chain
2pp8 Chain A Residue 1510 [
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Receptor-Ligand Complex Structure
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PDB
2pp8
Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules.
Resolution
1.5 Å
Binding residue
(original residue number in PDB)
G140 M141 P143 W144 Y203
Binding residue
(residue number reindexed from 1)
G137 M138 P140 W141 Y200
Annotation score
1
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
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Molecular Function
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Cellular Component
External links
PDB
RCSB:2pp8
,
PDBe:2pp8
,
PDBj:2pp8
PDBsum
2pp8
PubMed
18358002
UniProt
P38501
|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)
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