Structure of PDB 6syy Chain A Binding Site BS04
Receptor Information
>6syy Chain A (length=456) Species:
63363
(Aquifex aeolicus) [
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LSKQSLNIPGYFLFPDGQRVSITAKWTTLEVIPGKSTDMLVYEIDNEYNP
VIFLRKGQTFSADFVNNSGEDSIIHWHGFRAPWKSDGHPYYAVKDGETYS
YPDFTIIDRSGTYFYHPHPHGRTGYQVYYGLAGMIIIEDEDEDNLKQALD
LEYGVIDIPLIIQDKTFDSSGQLVYNPMGHMGFWGDTILVNLTPNPYMDV
ERKIYRFRILNGSNARPYRLALLRGNQRMRFWVIGVEGGLLDTPKEVNEI
LVAPGERIDILVDFRDASVNDVIKLYNFPHNLIMADNSEFEVMEFRVTKD
SAYDKSIPQRLSEVTPINTDGAQVQRITLGMRRMVFTINGETWEDGYANP
QDINNPKVLFEQNNGDVVIIEYVNNTGMYHPMHIHGFQFQVLERSLGPLR
ATDLGWKDTVIVAPMETVRIAVDMSHPYNEHQIYLLHCHILEHHDEGMMV
NYRVNA
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
6syy Chain A Residue 704 [
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Receptor-Ligand Complex Structure
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PDB
6syy
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis
Resolution
1.794 Å
Binding residue
(original residue number in PDB)
H120 H159 H510
Binding residue
(residue number reindexed from 1)
H77 H116 H439
Annotation score
3
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0005507
copper ion binding
GO:0016491
oxidoreductase activity
GO:0046872
metal ion binding
Biological Process
GO:0051301
cell division
Cellular Component
GO:0030288
outer membrane-bounded periplasmic space
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6syy
,
PDBe:6syy
,
PDBj:6syy
PDBsum
6syy
PubMed
UniProt
O67206
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