Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4EV2

Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine

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	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
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	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
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	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
C	0046872	molecular_function	metal ion binding
C	0048038	molecular_function	quinone binding
D	0005507	molecular_function	copper ion binding
D	0005777	cellular_component	peroxisome
D	0008131	molecular_function	primary methylamine oxidase activity
D	0009308	biological_process	amine metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
D	0046872	molecular_function	metal ion binding
D	0048038	molecular_function	quinone binding
E	0005507	molecular_function	copper ion binding
E	0005777	cellular_component	peroxisome
E	0008131	molecular_function	primary methylamine oxidase activity
E	0009308	biological_process	amine metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
E	0046872	molecular_function	metal ion binding
E	0048038	molecular_function	quinone binding
F	0005507	molecular_function	copper ion binding
F	0005777	cellular_component	peroxisome
F	0008131	molecular_function	primary methylamine oxidase activity
F	0009308	biological_process	amine metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
F	0046872	molecular_function	metal ion binding
F	0048038	molecular_function	quinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 701

Chain	Residue
A	LYS561
A	ASP593
A	HOH822
A	HOH1227
C	TYR160
C	LYS561
C	SER591
C	HOH1007

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 702

Chain	Residue
A	HIS458
A	HIS624
A	PEO707
A	HIS456

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 703

Chain	Residue
A	HIS23
A	TYR64
A	LYS68
A	VAL258
A	LYS265
A	ASP280
A	HOH936

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 704

Chain	Residue
A	HIS218
A	LYS219

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 705

Chain	Residue
A	GLU368
A	LYS393
A	ASP422
A	ARG424
A	HOH1117

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 706

Chain	Residue
A	PRO484
A	HOH1188
A	HOH1275
A	HOH1310

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEO A 707

Chain	Residue
A	TYQ405
A	LEU429
A	HIS456
A	HIS458
A	HIS624
A	MET634
A	CU702
A	HOH1365

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NEH A 708

Chain	Residue
A	TRP156
A	ALA317
A	ASP319
A	TYR323
A	TYQ405

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 701

Chain	Residue
B	LEU558
B	LYS561
B	SER591
B	HOH827
B	HOH1407
F	LYS561
F	ASP593

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 702

Chain	Residue
B	HIS456
B	HIS458
B	HIS624
B	PEO708

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 703

Chain	Residue
B	GLU368
B	LYS393
B	ASP422

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 704

Chain	Residue
B	HIS23
B	TYR64
B	LYS68
B	LYS265
B	ASP280
B	HOH1059
B	HOH1146

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 705

Chain	Residue
A	PRO442

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 706

Chain	Residue
B	ARG213
B	LYS214
B	VAL215
B	ASP436
B	HOH1305
B	HOH1363

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 707

Chain	Residue
A	TYR534
B	HIS218
B	LYS219
B	TYR448
B	PRO449
B	HOH1450
E	GLU69
E	GLN70

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEO B 708

Chain	Residue
B	TYQ405
B	HIS456
B	HIS458
B	HIS624
B	MET634
B	CU702
B	HOH839

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NEH B 709

Chain	Residue
B	TRP156
B	ALA317
B	ASP319
B	TYR323
B	TYQ405
B	HOH1308

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 710

Chain	Residue
B	VAL250
B	PHE252
B	LYS253
B	MET254
B	HIS343

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 701

Chain	Residue
C	HIS624
C	HOH1225
C	HOH1332
C	HIS456
C	HIS458

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 702

Chain	Residue
C	HIS23
C	TYR64
C	LYS68
C	LYS265
C	ASP280
C	HOH1279

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 703

Chain	Residue
C	LYS393
C	TYR410
C	ARG420
C	ASP422
C	ARG424
C	HOH1142

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 704

Chain	Residue
C	ARG213
C	LYS214
C	VAL215
C	ASP436
C	HOH979
C	HOH1072

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 705

Chain	Residue
C	GLU147
C	TYR177
C	SER216

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 706

Chain	Residue
C	PRO484
D	TRP443

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 707

Chain	Residue
C	ASN514
C	PRO550
C	LEU551
C	SER567
C	HOH916

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NEH C 708

Chain	Residue
C	TRP156
C	ALA317
C	ASP319
C	TYR323
C	ALA402
C	ALA403
C	TYQ405

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 709

Chain	Residue
C	HIS218
C	LYS219
C	HOH1228

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 701

Chain	Residue
D	HIS456
D	HIS458
D	HIS624
D	HOH1291

site_id	DC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 702

Chain	Residue
D	HIS23
D	TYR64
D	LYS68
D	LYS265
D	PHE266
D	HIS267
D	ASP280
D	HOH1077

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 703

Chain	Residue
D	LEU512
D	ASN514
D	GLU516
D	ARG521
D	HOH1239

site_id	DC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL D 704

Chain	Residue
D	HOH1173

site_id	DC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 705

Chain	Residue
D	ILE342
D	HIS343

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NEH D 706

Chain	Residue
D	ALA317
D	ASP319
D	TYR323
D	ALA402
D	TYQ405
D	HOH1202

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU E 701

Chain	Residue
E	HIS456
E	HIS458
E	HIS624
E	PEO706
E	HOH1127

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 702

Chain	Residue
E	GLU368
E	LYS393
E	TYR410
E	ASP422
E	ARG424
E	HOH932

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL E 703

Chain	Residue
E	HOH970
E	HOH1031
E	HOH1272

site_id	EC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 704

Chain	Residue
E	HIS23
E	TYR64
E	LYS68
E	LYS265
E	ASP280
E	HOH929

site_id	EC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 705

Chain	Residue
E	GLU58
E	PRO59
E	TYR575
E	ASN578
E	LEU580
E	HOH923
E	HOH950
E	HOH1020

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEO E 706

Chain	Residue
E	TYQ405
E	HIS456
E	MET634
E	CU701
E	HOH1045

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NEH E 707

Chain	Residue
E	ALA317
E	ASP319
E	TYR323
E	TYQ405

site_id	EC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU F 701

Chain	Residue
F	HIS456
F	HIS458
F	HIS624
F	PEO707

site_id	EC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 702

Chain	Residue
F	HIS23
F	TYR64
F	LYS68
F	VAL258
F	LYS265
F	ASP280
F	HOH1298

site_id	EC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 703

Chain	Residue
F	GLU58
F	PRO59
F	HIS294
F	TYR575
F	ASN578
F	HOH890
F	HOH924
F	HOH988

site_id	EC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL F 704

Chain	Residue
E	GLY371
F	LYS393
F	ASP422
F	ARG424
F	HOH1256

site_id	EC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 705

Chain	Residue
F	ARG213
F	LYS214
F	VAL215
F	ASP436
F	ASN450
F	HOH1220

site_id	FC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL F 706

Chain	Residue
E	PRO442
F	TYR485
F	HOH1101

site_id	FC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEO F 707

Chain	Residue
F	TYQ405
F	HIS456
F	HIS458
F	HIS624
F	MET634
F	CU701
F	HOH1125

site_id	FC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NEH F 708

Chain	Residue
F	TRP156
F	ALA317
F	ASP319
F	TYR323
F	ALA403
F	TYQ405

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	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OOV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N9H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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