Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8S1Z

Crystal structure of glycosylated human primary amine oxidase AOC3

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005769	cellular_component	early endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0005886	cellular_component	plasma membrane
A	0005902	cellular_component	microvillus
A	0006954	biological_process	inflammatory response
A	0007155	biological_process	cell adhesion
A	0008131	molecular_function	primary methylamine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0009986	cellular_component	cell surface
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0048038	molecular_function	quinone binding
B	0005507	molecular_function	copper ion binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005769	cellular_component	early endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005794	cellular_component	Golgi apparatus
B	0005886	cellular_component	plasma membrane
B	0005902	cellular_component	microvillus
B	0006954	biological_process	inflammatory response
B	0007155	biological_process	cell adhesion
B	0008131	molecular_function	primary methylamine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0009986	cellular_component	cell surface
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	0048038	molecular_function	quinone binding
C	0005507	molecular_function	copper ion binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005769	cellular_component	early endosome
C	0005783	cellular_component	endoplasmic reticulum
C	0005794	cellular_component	Golgi apparatus
C	0005886	cellular_component	plasma membrane
C	0005902	cellular_component	microvillus
C	0006954	biological_process	inflammatory response
C	0007155	biological_process	cell adhesion
C	0008131	molecular_function	primary methylamine oxidase activity
C	0009308	biological_process	amine metabolic process
C	0009986	cellular_component	cell surface
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0046982	molecular_function	protein heterodimerization activity
C	0048038	molecular_function	quinone binding
D	0005507	molecular_function	copper ion binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005769	cellular_component	early endosome
D	0005783	cellular_component	endoplasmic reticulum
D	0005794	cellular_component	Golgi apparatus
D	0005886	cellular_component	plasma membrane
D	0005902	cellular_component	microvillus
D	0006954	biological_process	inflammatory response
D	0007155	biological_process	cell adhesion
D	0008131	molecular_function	primary methylamine oxidase activity
D	0009308	biological_process	amine metabolic process
D	0009986	cellular_component	cell surface
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0046982	molecular_function	protein heterodimerization activity
D	0048038	molecular_function	quinone binding

Functional Information from PROSITE/UniProt

site_id	PS01164
Number of Residues	14
Details	COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrsmsTllNYDY

Chain	Residue	Details
A	LEU460-TYR473

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

Chain	Residue	Details
A	THR679-PRO692

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P19801","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1US1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1US1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PU4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1US1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1US1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BTY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24304424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BTY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"16046623","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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