1TU5

Crystal structure of bovine plasma copper-containing amine oxidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005576	cellular_component	extracellular region
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	0006954	biological_process	inflammatory response
A	0008131	molecular_function	primary methylamine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048038	molecular_function	quinone binding
B	0005507	molecular_function	copper ion binding
B	0005576	cellular_component	extracellular region
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	0006954	biological_process	inflammatory response
B	0008131	molecular_function	primary methylamine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	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. LVFrsvsTmlNYDY

Chain	Residue	Details
A	LEU459-TYR472

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

Chain	Residue	Details
A	THR678-PRO691

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801

Chain	Residue	Details
A	ASP385
B	ASP385

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0007744|PDB:2PNC

Chain	Residue	Details
A	TPQ470
B	TPQ470

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744|PDB:2PNC

Chain	Residue	Details
A	TYR383
A	MET467
B	TYR383
B	MET467

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC

Chain	Residue	Details
A	HIS519
A	HIS521
A	HIS683
B	HIS519
B	HIS521
B	HIS683

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	BINDING: BINDING => ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC

Chain	Residue	Details
A	ASP528
B	ASP528
B	LEU529
B	ASP530
B	GLU571
B	PHE662
B	ASN664
B	GLU666
B	ASP672
B	LEU673
A	LEU529
A	ASP530
A	GLU571
A	PHE662
A	ASN664
A	GLU666
A	ASP672
A	LEU673

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0007744|PDB:1TU5

Chain	Residue	Details
A	TPQ470
B	TPQ470

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC

Chain	Residue	Details
A	ASN136
B	ASN136

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5

Chain	Residue	Details
A	ASN231
A	ASN665
B	ASN231
B	ASN665

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
A	ASP385

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
B	ASP385

---