Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NBJ

Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005777	cellular_component	peroxisome
A	0008131	molecular_function	primary methylamine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A	0046872	molecular_function	metal ion binding
A	0048038	molecular_function	quinone binding
B	0005507	molecular_function	copper ion binding
B	0005777	cellular_component	peroxisome
B	0008131	molecular_function	primary methylamine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B	0046872	molecular_function	metal ion binding
B	0048038	molecular_function	quinone binding
C	0005507	molecular_function	copper ion binding
C	0005777	cellular_component	peroxisome
C	0008131	molecular_function	primary methylamine oxidase activity
C	0009308	biological_process	amine metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
C	0046872	molecular_function	metal ion binding
C	0048038	molecular_function	quinone binding
D	0005507	molecular_function	copper ion binding
D	0005777	cellular_component	peroxisome
D	0008131	molecular_function	primary methylamine oxidase activity
D	0009308	biological_process	amine metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
D	0046872	molecular_function	metal ion binding
D	0048038	molecular_function	quinone binding
E	0005507	molecular_function	copper ion binding
E	0005777	cellular_component	peroxisome
E	0008131	molecular_function	primary methylamine oxidase activity
E	0009308	biological_process	amine metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
E	0046872	molecular_function	metal ion binding
E	0048038	molecular_function	quinone binding
F	0005507	molecular_function	copper ion binding
F	0005777	cellular_component	peroxisome
F	0008131	molecular_function	primary methylamine oxidase activity
F	0009308	biological_process	amine metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
F	0046872	molecular_function	metal ion binding
F	0048038	molecular_function	quinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 701

Chain	Residue
A	TY8405
A	HIS456
A	HIS458
A	HIS624

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 702

Chain	Residue
A	PRO209
A	ASN210
A	ARG211
A	HOH1250
A	HOH1373

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 A 703

Chain	Residue
A	HIS218
A	LYS219

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 704

Chain	Residue
A	GLY594
A	VAL595
A	ARG596
A	HOH1324
A	HOH1393

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 701

Chain	Residue
B	TY8405
B	HIS456
B	HIS458
B	HIS624

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 702

Chain	Residue
B	PRO209
B	ASN210
B	ARG211
B	HOH1250
B	HOH1373

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 703

Chain	Residue
B	HIS218
B	LYS219

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 704

Chain	Residue
B	GLY594
B	VAL595
B	ARG596
B	HOH1324
B	HOH1393

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 701

Chain	Residue
C	TY8405
C	HIS456
C	HIS458
C	HIS624

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 702

Chain	Residue
C	PRO209
C	ASN210
C	ARG211
C	HOH1250
C	HOH1373

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 C 703

Chain	Residue
C	HIS218
C	LYS219

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 704

Chain	Residue
C	GLY594
C	VAL595
C	ARG596
C	HOH1324
C	HOH1393

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 701

Chain	Residue
D	TY8405
D	HIS456
D	HIS458
D	HIS624

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 702

Chain	Residue
D	PRO209
D	ASN210
D	ARG211
D	HOH1250
D	HOH1373

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 703

Chain	Residue
D	HIS218
D	LYS219

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 704

Chain	Residue
D	GLY594
D	VAL595
D	ARG596
D	HOH1324
D	HOH1393

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU E 701

Chain	Residue
E	TY8405
E	HIS456
E	HIS458
E	HIS624

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 702

Chain	Residue
E	PRO209
E	ASN210
E	ARG211
E	HOH1250
E	HOH1373

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 E 703

Chain	Residue
E	HIS218
E	LYS219

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 704

Chain	Residue
E	GLY594
E	VAL595
E	ARG596
E	HOH1324
E	HOH1393

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU F 701

Chain	Residue
F	TY8405
F	HIS456
F	HIS458
F	HIS624

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 702

Chain	Residue
F	PRO209
F	ASN210
F	ARG211
F	HOH1250
F	HOH1373

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 F 703

Chain	Residue
F	HIS218
F	LYS219

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 704

Chain	Residue
F	GLY594
F	VAL595
F	ARG596
F	HOH1324
F	HOH1393

Functional Information from PROSITE/UniProt

site_id	PS01159
Number of Residues	26
Details	WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP

Chain	Residue	Details
A	TRP164-PRO189

site_id	PS01165
Number of Residues	14
Details	COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP

Chain	Residue	Details
A	THR619-PRO632

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OOV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N9H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)