Structure of PDB 3oma Chain D Binding Site BS03
Receptor Information
>3oma Chain D (length=256) Species:
272943
(Cereibacter sphaeroides 2.4.1) [
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LEIIGRPQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYA
VWRFHEKRNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFNQQEI
PEADVTVKVTGYQWYWGYEYPDEEISFESYMIGSPATGGDNRMSPEVEQQ
LIEAGYSRDEFLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQD
AVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL
EQHHHH
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
3oma Chain D Residue 286 [
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Receptor-Ligand Complex Structure
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PDB
3oma
Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
C252 E254 C256 H260
Binding residue
(residue number reindexed from 1)
C223 E225 C227 H231
Annotation score
1
Enzymatic activity
Enzyme Commision number
7.1.1.9
: cytochrome-c oxidase.
Gene Ontology
Molecular Function
GO:0004129
cytochrome-c oxidase activity
GO:0005507
copper ion binding
GO:0016491
oxidoreductase activity
GO:0046872
metal ion binding
Biological Process
GO:0022900
electron transport chain
GO:0042773
ATP synthesis coupled electron transport
GO:1902600
proton transmembrane transport
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:3oma
,
PDBe:3oma
,
PDBj:3oma
PDBsum
3oma
PubMed
21205904
UniProt
Q3J5G0
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