3NSY

The multi-copper oxidase CueO with six Met to Ser mutations (M358S,M361S,M362S,M364S,M366S,M368S)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0005507	molecular_function	copper ion binding
A	0010273	biological_process	detoxification of copper ion
A	0016491	molecular_function	oxidoreductase activity
A	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
A	0016724	molecular_function	oxidoreductase activity, acting on metal ions, oxygen as acceptor
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046688	biological_process	response to copper ion
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 604

Chain	Residue
A	HIS443
A	CYS500
A	HIS505
A	MET510

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU A 601

Chain	Residue
A	C2O602
A	HOH17
A	HIS101
A	HIS103
A	HIS446
A	HIS448

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O A 602

Chain	Residue
A	HIS101
A	HIS103
A	HIS141
A	HIS143
A	HIS446
A	HIS448
A	HIS499
A	HIS501
A	CU601

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 605

Chain	Residue
A	MET355
A	ASP360
A	ASP439
A	MET441

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site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 606

Chain	Residue
A	HIS488
A	HOH804
A	HOH813

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Functional Information from PROSITE/UniProt

site_id	PS00080
Number of Residues	12
Details	MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHlleHedtGM

Chain	Residue	Details
A	HIS499-MET510

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site_id	PS00152
Number of Residues	10
Details	ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PSLDSSGSQS

Chain	Residue	Details
A	PRO357-SER366

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: type 2 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW

Chain	Residue	Details
A	HIS101
A	HIS446

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW

Chain	Residue	Details
A	HIS103
A	HIS141
A	HIS143
A	HIS448
A	HIS499
A	HIS501

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW

Chain	Residue	Details
A	HIS505
A	HIS443
A	CYS500

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