Structure of PDB 5n4l Chain A Binding Site BS03

Receptor Information
>5n4l Chain A (length=1034) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
REKHYYIGITEAVWDYASGSEEKELISVDTEQSNFYLRNGPDRIGRKYKK
ALYSEYTDGTFTKTIDKPAWLGLLGPVIKAEVGDKVSVHVKNFASRPYTF
HAHGVTYTKANEGAIYPDNTTDFQRADDKLFPGQQYLYVLRANEPSPGEG
DSNCVTRIYHSHVDAPKDIASGLIGPLILCKKGSLHKEKEENIDQEFVLM
FSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSL
PGLSMCAEDRVKWYLFGMGNEVDVHSALFHGQALTSKNYHTDIINLFPAT
LIDVSMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRDCNKPSPDDDIQDRH
VRHYYIAAEETIWDYAPSGTDTFTGENLTSLGSDSRVFFEQGATRIGGSY
KKLVYREYTDDSFTNRKQRGPDEEHLGILGPVIWAEVGDIIRVTFHNKGQ
FPLSIQPMGVRFTKENEGTYYGPDGRSSKQASHVAPKETFTYEWTVPKEM
GPTYADPVCLSKMYYSGVDLTKDIFTGLIGPMKICKKGSLLADGRQKDVD
KEFYLFATVFDENESLLLDDNIRMFTTAPENVDKEDEDFQESNKMHSMNG
FMYGNLPGLNMCLGESIVWYLFSAGNEADVHGIYFSGNTYLSKGERRDTA
NLFPHKSLTLLMTPDTEGSFDVECLTTDHYTGGMKQKYTVNQCKGQFEDV
TLYQGERTYYIAAVEVEWDYSPSRDWEMELHHLQEQNVSNAFLDKEEFFI
GSKYKKVVYREFTDSTFREQVKRRAEEEHLGILGPLIHADVGDKVKVVFK
NMASRPYSIHAHGVKTKSSTVAPTLPGEVRTYIWQIPERSGAGTEDSPCI
PWAYYSTVDRVKDLYSGLIGPLIVCRKSYVKVFNPKKKMEFSLLFLVFDE
NESWYLDDNINTYSDHPEKVNKDNEEFIESNKMHAINGKMFGNLQGLTMH
VGDEVNWYVMAMGNEIDLHTVHFHGHSFQYKHRGIHSSDVFDLFPGTYQT
LEMFPQTPGTWLLHCHVTDHIHAGMVTTYTVLPN
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 chain5n4l Chain A Residue 1103 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5n4l Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		H275 C318 H323
Binding residue
(residue number reindexed from 1)		H275 C318 H323
Annotation score1
Enzymatic activity
Enzyme Commision number 1.11.1.27: glutathione-dependent peroxiredoxin.
1.11.1.9: glutathione peroxidase.
1.16.3.1: ferroxidase.
1.16.3.4: cuproxidase.
Gene Ontology
Molecular Function
GO:0004322 ferroxidase activity
GO:0004602 glutathione peroxidase activity
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0016724 oxidoreductase activity, acting on metal ions, oxygen as acceptor
GO:0046872 metal ion binding
GO:0047066 phospholipid-hydroperoxide glutathione peroxidase activity
GO:0051087 protein-folding chaperone binding
Biological Process
GO:0001889 liver development
GO:0006826 iron ion transport
GO:0006878 intracellular copper ion homeostasis
GO:0006879 intracellular iron ion homeostasis
GO:0007565 female pregnancy
GO:0007584 response to nutrient
GO:0007595 lactation
GO:0015679 plasma membrane copper ion transport
GO:0030324 lung development
GO:0046688 response to copper ion
GO:0060056 mammary gland involution
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0009986 cell surface

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5n4l, PDBe:5n4l, PDBj:5n4l
PDBsum5n4l
PubMed29177316
UniProtP13635|CERU_RAT Ceruloplasmin (Gene Name=Cp)

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