Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3T0U

Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I)

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 amine 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 amine 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 amine 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	5
Details	BINDING SITE FOR RESIDUE CU1 A 801

Chain	Residue
A	TYR405
A	LEU425
A	HIS456
A	HIS458
A	HIS624

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 802

Chain	Residue
A	ASP280
A	HOH1162
A	HIS23
A	TYR64
A	LYS68
A	LYS265

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	PRO484
A	TYR485
A	TYR499
A	HOH1413

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 804

Chain	Residue
A	TRP67
A	LYS68

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 805

Chain	Residue
A	LYS393
A	ARG420
A	ASP422
A	ARG424
A	HOH969
A	HOH1158
A	HOH1300
A	HOH1516
B	GLY371

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 806

Chain	Residue
A	LYS561
A	LYS561
A	SER591
A	ASP593
A	HOH1241
A	HOH1241

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 801

Chain	Residue
B	TYR405
B	LEU425
B	HIS456
B	HIS458
B	HIS624

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 802

Chain	Residue
B	TYR534
B	HOH1001
B	HOH1461
C	GLN66
C	GLN70
C	GLY72

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 803

Chain	Residue
B	HIS23
B	TYR64
B	LYS68
B	LYS265
B	ASP280
B	HOH1065
B	HOH1692

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 804

Chain	Residue
B	HIS218
B	LYS219

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 805

Chain	Residue
C	TRP67

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 806

Chain	Residue
B	LYS214
B	VAL215
B	ASP436
B	HOH1307

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 807

Chain	Residue
A	PRO442
B	PRO484
B	TYR485
B	HOH1371
B	HOH1424

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 808

Chain	Residue
B	LYS561
B	SER591
B	HOH1392
C	LYS561
C	ASP593
C	GOL805
C	HOH1022

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 C 801

Chain	Residue
C	TYR405
C	HIS456
C	HIS458
C	HIS624

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 802

Chain	Residue
C	PRO442
C	PRO484
C	TYR485
C	HOH1424
C	HOH1656

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 803

Chain	Residue
A	HOH1432
C	ARG61
C	LYS62
C	GLN70
C	ASP471
C	ASP613
C	HOH1648
C	HOH1783
C	HOH1798

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 804

Chain	Residue
C	GLY371
C	LYS393
C	VAL412
C	ASP422
C	ARG424
C	HOH923
C	HOH1110
C	HOH1765

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 805

Chain	Residue
C	SER591
C	HOH1022
C	HOH1333
B	LYS561
B	ASP593
B	GOL808
C	LYS561

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 806

Chain	Residue
C	HIS23
C	TYR64
C	LYS68
C	LYS265
C	ASP280
C	HOH1092

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 807

Chain	Residue
C	HIS218
C	LYS219
C	TYR448
C	TYR534

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 808

Chain	Residue
C	LYS214
C	VAL215
C	GLY435
C	ASP436

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 809

Chain	Residue
C	GLY142
C	PRO144
C	GLU147
C	TYR177
C	HOH1258

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
B	HIS456
B	HIS458
B	HIS624
C	HIS456
C	HIS458
C	HIS624
A	HIS456
A	HIS458
A	HIS624

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

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

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