3SX1

Hansenula polymorpha copper amine oxidase-1 in its apo form

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	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	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	0046872	molecular_function	metal ion binding
B	0048038	molecular_function	quinone binding
B	0052595	molecular_function	aliphatic amine oxidase activity
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	0046872	molecular_function	metal ion binding
C	0048038	molecular_function	quinone binding
C	0052595	molecular_function	aliphatic amine oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 693

Chain	Residue
C	HIS23
C	TYR64
C	LYS68
C	LYS265
C	ASP280
C	HOH989
C	HOH1975
C	HOH2352

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 693

Chain	Residue
A	LYS219
A	TYR448
A	TYR534
A	HIS218

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 693

Chain	Residue
B	HIS23
B	TYR64
B	LYS68
B	LYS265
B	ASP280
B	HOH724

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 694

Chain	Residue
B	ARG163
B	PHE310
B	HOH917
B	HOH1248
B	HOH2873
C	HOH765

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 694

Chain	Residue
A	PRO442
A	PRO484
A	TYR485
A	HOH852
A	HOH2150
A	HOH2814

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 694

Chain	Residue
C	ARG213
C	LYS214
C	VAL215
C	GLY435
C	ASP436
C	ASN450
C	HOH836
C	HOH1101

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 695

Chain	Residue
A	ARG211
A	LYS214
A	VAL215
A	GLY435
A	ASP436

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 695

Chain	Residue
A	GLN70
B	HIS218
B	LYS219
B	TYR448
B	PRO449
B	HOH1040
C	TYR534

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 696

Chain	Residue
A	GLN66
A	GLN70
A	GLY72
A	HOH2485
C	TYR534
C	THR650
C	HOH750

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 696

Chain	Residue
B	PRO484
B	TYR485
B	TYR499
B	HOH1622

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 695

Chain	Residue
C	PRO484
C	TYR485

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 696

Chain	Residue
C	ARG20
C	HIS218
C	LYS219

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 697

Chain	Residue
B	PRO442
B	HOH2980
C	PRO484

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 697

Chain	Residue
A	TRP67
A	LYS68
A	HOH2024

---

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 698

Chain	Residue
A	GLY142
A	GLU147
A	TYR177
A	HOH792
A	HOH908
B	HOH2841

---

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

Chain	Residue	Details
A	LEU394-TYR407

---

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	3
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552

Chain	Residue	Details
A	ASP319
B	ASP319
C	ASP319

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF

Chain	Residue	Details
A	TYR405
B	TYR405
C	TYR405

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5

Chain	Residue	Details
A	ALA317
B	ALA317
C	ALA317

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P46883

Chain	Residue	Details
A	ALA402
B	ALA402
C	ALA402

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF

Chain	Residue	Details
A	HIS456
A	HIS458
A	HIS624
B	HIS456
B	HIS458
B	HIS624
C	HIS456
C	HIS458
C	HIS624

---

site_id	SWS_FT_FI6
Number of Residues	9
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q43077

Chain	Residue	Details
A	ASP465
A	ASP613
A	ILE614
B	ASP465
B	ASP613
B	ILE614
C	ASP465
C	ASP613
C	ILE614

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE

Chain	Residue	Details
A	TYR405
B	TYR405
C	TYR405

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552

Chain	Residue	Details
A	ASN243
B	ASN243
C	ASN243

---