Structure of PDB 1m57 Chain H Binding Site BS01

Receptor Information
>1m57 Chain H (length=260) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LEIIGRPQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYA
VWRFHEKRNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFNQQEI
PEADVTVKVTGYQWYWGYEYPDEEISFESYMIGSPATGGDNRMSPEVEQQ
LIEAGYSRDEFLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQD
AVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWL
EQARGGTYEL
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1m57 Chain H Residue 1003 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1m57 The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		C252 C256 H260
Binding residue
(residue number reindexed from 1)		C223 C227 H231
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:0005515 protein 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:1m57, PDBe:1m57, PDBj:1m57
PDBsum1m57
PubMed12144789
UniProtQ03736|COX2_CERSP Cytochrome c oxidase subunit 2 (Gene Name=ctaC)

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