Structure of PDB 3nsc Chain A

Receptor sequence

>3nscA (length=470) Species: 562 (Escherichia coli)

ERPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYNGNLLGPAVK
LQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTL
NVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGID
DVPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRG
WLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGE
RFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGA
LPDTLSSLPALPSLEGLTVRKLQLSMDPMLDMMGMQMLMEKYGDQAMAGM
DFHHANKINGQAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQF
RILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHSHL
LEHEDTGMMLGFTVLQGDHG

3D structure

• PDB: 3nsc Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence.
• Chain: A
• Resolution: 1.5 Å

Enzymatic activity

• Enzyme Commision number: 1.16.3.4: cuproxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CU	A	H103 H141 H501	H74 H112 H449
BS02	CU	A	H101 H446 H448	H72 H394 H396
BS03	CU	A	H143 H448 H499	H114 H396 H447

Gene Ontology

Molecular Function

• GO:0004322 ferroxidase activity
• GO:0005507 copper ion binding
• GO:0016491 oxidoreductase activity
• GO:0016682 oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
• GO:0016722 oxidoreductase activity, acting on metal ions
• GO:0016724 oxidoreductase activity, acting on metal ions, oxygen as acceptor
• GO:0046872 metal ion binding

Biological Process

• GO:0010273 detoxification of copper ion
• GO:0046688 response to copper ion

Cellular Component

• GO:0030288 outer membrane-bounded periplasmic space
• GO:0042597 periplasmic space

External links

• PDB: RCSB:3nsc, PDBe:3nsc, PDBj:3nsc
• PDBsum: 3nsc
• PubMed: 21903583
• UniProt: P36649|CUEO_ECOLI Multicopper oxidase CueO (Gene Name=cueO)