Structure of PDB 2yev Chain E Binding Site BS02

Receptor Information
>2yev Chain E (length=319) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AHRVAITHPGGSFNQEVAFLFPWVYFFSFLIFLVVAGSLAYVTWKFRARP
EDQEEPPQIHGNDRLEVVWTLIPLAIVFVLFGLTAKALIQVNRPIPGAMK
VEVTGYQFWWDFHYPELGLRNSNELVLPAGVPVELEITSKDVIHSFWVPG
LAGKRDAIPGQTTRISFEPKEPGLYYGFCAELCGASHARMLFRVVVLPKE
EFDRFVEAAKASPAPVADERGQQVFQQNCAACHGVARSMPPAVIGPELGL
WGNRTSLGAGIVENTPENLKAWIRDPAGMKPGVKMPGFPQLSEEDLDALV
RYLEGLKVEGFDFGALPKF
Ligand information
Ligand IDCUA
InChIInChI=1S/2Cu
InChIKeyALKZAGKDWUSJED-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Cu][Cu]
FormulaCu2
NameDINUCLEAR COPPER ION
ChEMBL
DrugBank
ZINC
PDB chain2yev Chain E Residue 585 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2yev Structural Insights Into Electron Transfer in Caa3-Type Cytochrome Oxidases.
Resolution2.36 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 score1
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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Biological Process

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Cellular Component
External links
PDB RCSB:2yev, PDBe:2yev, PDBj:2yev
PDBsum2yev
PubMed22763450
UniProtQ5SLI2

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