Structure of PDB 1as8 Chain A Binding Site BS02
Receptor Information
>1as8 Chain A (length=336) Species:
511
(Alcaligenes faecalis) [
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ATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVID
DAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAAT
GALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGA
IMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAY
EDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTR
PHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAY
VNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG
Ligand information
Ligand ID
CU
InChI
InChI=1S/Cu/q+2
InChIKey
JPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341
[Cu++]
Formula
Cu
Name
COPPER (II) ION
ChEMBL
DrugBank
DB14552
ZINC
PDB chain
1as8 Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
1as8
Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications.
Resolution
1.85 Å
Binding residue
(original residue number in PDB)
H100 H135
Binding residue
(residue number reindexed from 1)
H97 H132
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1as8
,
PDBe:1as8
,
PDBj:1as8
PDBsum
1as8
PubMed
9353305
UniProt
P38501
|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)
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