5ZP9

Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at pH 6 at 283 K (1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
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
A	0052595	molecular_function	aliphatic amine oxidase activity
B	0005507	molecular_function	copper ion binding
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
B	0052595	molecular_function	aliphatic amine oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CU A 1001

Chain	Residue
A	TYQ382
A	HIS431
A	HIS433
A	HIS592
A	HOH1251
A	HOH1490

---

site_id	AC2
Number of Residues	5
Details	binding site for residue NA A 1002

Chain	Residue
A	ILE582
A	HOH1304
A	ASP440
A	MET441
A	ASP581

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CU B 701

Chain	Residue
B	TYQ382
B	HIS431
B	HIS433
B	HIS592
B	HOH1016
B	HOH1235

---

site_id	AC4
Number of Residues	5
Details	binding site for residue NA B 702

Chain	Residue
B	ASP440
B	MET441
B	ASP581
B	ILE582
B	HOH1024

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET371-TYR384

---

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

Chain	Residue	Details
A	THR587-PRO600

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807

Chain	Residue	Details
A	ASP298
B	ASP298

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807

Chain	Residue	Details
A	TYQ382
B	TYQ382

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P12807

Chain	Residue	Details
A	TYR296
B	TYR296

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P46883

Chain	Residue	Details
A	ILE379
B	ILE379

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:9405045, ECO:0007744|PDB:1AV4, ECO:0007744|PDB:1AVL, ECO:0007744|PDB:1IU7, ECO:0007744|PDB:1IVU, ECO:0007744|PDB:1IVV, ECO:0007744|PDB:1IVW, ECO:0007744|PDB:1IVX, ECO:0007744|PDB:1RJO, ECO:0007744|PDB:1SIH, ECO:0007744|PDB:1SII, ECO:0007744|PDB:1UI8, ECO:0007744|PDB:1W4N, ECO:0007744|PDB:1W5Z, ECO:0007744|PDB:1W6C, ECO:0007744|PDB:1W6G, ECO:0007744|PDB:2BT3, ECO:0007744|PDB:2CFD, ECO:0007744|PDB:2CFG, ECO:0007744|PDB:2CFK, ECO:0007744|PDB:2CFL, ECO:0007744|PDB:2CFW, ECO:0007744|PDB:2CG0, ECO:0007744|PDB:2CG1, ECO:0007744|PDB:2CWT, ECO:0007744|PDB:2CWU, ECO:0007744|PDB:2CWV, ECO:0007744|PDB:2D1W, ECO:0007744|PDB:2E2T, ECO:0007744|PDB:2E2U, ECO:0007744|PDB:2E2V, ECO:0007744|PDB:2YX9, ECO:0007744|PDB:2ZL8, ECO:0007744|PDB:3AMO, ECO:0007744|PDB:3KII, ECO:0007744|PDB:3KN4, ECO:0007744|PDB:3WA2, ECO:0007744|PDB:3WA3

Chain	Residue	Details
A	HIS431
A	HIS433
A	HIS592
B	HIS431
B	HIS433
B	HIS592

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045

Chain	Residue	Details
A	TYQ382
B	TYQ382

---