Structure of PDB 3o0r Chain B Binding Site BS04
Receptor Information
>3o0r Chain B (length=449) Species:
208964
(Pseudomonas aeruginosa PAO1) [
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FASQAVAKPYFVFALILFVGQILFGLIMGLQYVVGDFLFPAIPFNVARMV
HTNLLIVWLLFGFMGAAYYLVPEESDCELYSPKLAWILFWVFAAAGVLTI
LGYLLVPYAGLARLTGNELWPTMGREFLEQPTISKAGIVIVALGFLFNVG
MTVLRGRKTAISMVLMTGLIGLALLFLFSFYNPENLTRDKFYWWWVVHLW
VEGVWELIMGAILAFVLVKITGVDREVIEKWLYVIIAMALISGIIGTGHH
YFWIGVPGYWLWLGSVFSALEPLPFFAMVLFAFNTINRRRRDYPNRAVAL
WAMGTTVMAFLGAGVWGFMHTLAPVNYYTHGTQLTAAHGHMAFYGAYAMI
VMTIISYAMPRLRGIGEAMDNRSQVLEMWGFWLMTVAMVFITLFLSAAGV
LQVWLQRMPADGAAMTFMATQDQLAIFYWLREGAGVVFLIGLVAYLLSF
Ligand information
Ligand ID
O
InChI
InChI=1S/H2O/h1H2
InChIKey
XLYOFNOQVPJJNP-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
O
CACTVS 3.341
[O]
Formula
O
Name
OXYGEN ATOM
ChEMBL
CHEMBL1098659
DrugBank
DB09145
ZINC
PDB chain
3o0r Chain B Residue 805 [
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Receptor-Ligand Complex Structure
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PDB
3o0r
Structural basis of biological N2O generation by bacterial nitric oxide reductase
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
E211 H259
Binding residue
(residue number reindexed from 1)
E202 H250
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.7.2.5
: nitric-oxide reductase (cytochrome c).
Gene Ontology
Molecular Function
GO:0004129
cytochrome-c oxidase activity
GO:0016491
oxidoreductase activity
GO:0016966
nitric oxide reductase activity
GO:0020037
heme binding
GO:0046872
metal ion binding
Biological Process
GO:0009060
aerobic respiration
GO:0015990
electron transport coupled proton transport
GO:0019333
denitrification pathway
GO:0022904
respiratory electron transport chain
Cellular Component
GO:0005886
plasma membrane
GO:0016020
membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3o0r
,
PDBe:3o0r
,
PDBj:3o0r
PDBsum
3o0r
PubMed
21109633
UniProt
Q59647
|NORB_PSEAE Nitric oxide reductase subunit B (Gene Name=norB)
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