Structure of PDB 2yev Chain E Binding Site BS02
Receptor Information
>2yev Chain E (length=319) Species:
300852
(Thermus thermophilus HB8) [
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AHRVAITHPGGSFNQEVAFLFPWVYFFSFLIFLVVAGSLAYVTWKFRARP
EDQEEPPQIHGNDRLEVVWTLIPLAIVFVLFGLTAKALIQVNRPIPGAMK
VEVTGYQFWWDFHYPELGLRNSNELVLPAGVPVELEITSKDVIHSFWVPG
LAGKRDAIPGQTTRISFEPKEPGLYYGFCAELCGASHARMLFRVVVLPKE
EFDRFVEAAKASPAPVADERGQQVFQQNCAACHGVARSMPPAVIGPELGL
WGNRTSLGAGIVENTPENLKAWIRDPAGMKPGVKMPGFPQLSEEDLDALV
RYLEGLKVEGFDFGALPKF
Ligand information
Ligand ID
CUA
InChI
InChI=1S/2Cu
InChIKey
ALKZAGKDWUSJED-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Cu][Cu]
Formula
Cu2
Name
DINUCLEAR COPPER ION
ChEMBL
DrugBank
ZINC
PDB chain
2yev Chain E Residue 585 [
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Receptor-Ligand Complex Structure
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PDB
2yev
Structural Insights Into Electron Transfer in Caa3-Type Cytochrome Oxidases.
Resolution
2.36 Å
Binding residue
(original residue number in PDB)
H162 C197 E199 C201 H205 M208
Binding residue
(residue number reindexed from 1)
H144 C179 E181 C183 H187 M190
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:0009055
electron transfer activity
GO:0016491
oxidoreductase activity
GO:0020037
heme binding
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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Cellular Component
External links
PDB
RCSB:2yev
,
PDBe:2yev
,
PDBj:2yev
PDBsum
2yev
PubMed
22763450
UniProt
Q5SLI2
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