Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SXX

Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)

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	7
Details	BINDING SITE FOR RESIDUE CO A 801

Chain	Residue
A	TYR405
A	LEU425
A	HIS456
A	HIS458
A	HIS624
A	HOH1628
A	HOH1736

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 802

Chain	Residue
A	VAL215
A	GLY435
A	ASP436
A	ASN450
A	HOH1031
A	HOH1083
A	ARG213
A	LYS214

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	GLU368
A	LYS393
A	TYR410
A	VAL412
A	ARG420
A	ASP422
A	ARG424
A	HOH1007
A	HOH1431
A	HOH1458
A	HOH1650
B	GLY371

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 804

Chain	Residue
A	ARG61
A	ILE65
A	ASP471
A	ASP613
A	HOH1303
A	HOH1326
A	HOH1589

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 805

Chain	Residue
A	GLN66
A	GLN70
A	GLY72
E	TYR448
F	TYR534
F	HOH912
F	HOH1875

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

Chain	Residue
A	PRO484
A	TYR485
A	TYR499
A	HOH1447
A	HOH1647
B	PRO442

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 807

Chain	Residue
A	HIS23
A	TYR64
A	LYS68
A	VAL258
A	LYS265
A	PHE266
A	ASP280
A	HOH920
A	HOH1490

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 808

Chain	Residue
A	HIS218
A	LYS219
A	TYR448
A	HOH1630
B	TYR534

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 809

Chain	Residue
A	ARG57
A	GLU93
A	GLY94
A	GLU105
A	ARG107
A	HOH1763
A	HOH1765

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 810

Chain	Residue
A	TYR160
A	LEU558
A	LYS561
A	SER591
A	HOH1903
F	LYS561
F	ASP593
F	GOL808
F	HOH1087

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 811

Chain	Residue
A	GLY142
A	PRO144
A	GLU147
A	TYR177
A	LYS217
A	HOH1295
E	HOH1647

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CO B 801

Chain	Residue
B	TYR405
B	LEU425
B	HIS456
B	HIS458
B	HIS624
B	HOH1629
B	HOH1736

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 802

Chain	Residue
B	ARG213
B	LYS214
B	VAL215
B	GLY435
B	ASP436
B	ASN450
B	HOH1025
B	HOH1663

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 803

Chain	Residue
B	GLU368
B	LYS393
B	TYR410
B	ASP422
B	HOH1005
B	HOH1125
B	HOH1462

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 804

Chain	Residue
A	PRO442
B	PRO484
B	TYR485
B	TYR499
B	HOH1501
B	HOH1826

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 805

Chain	Residue
B	HIS23
B	TYR64
B	LYS68
B	VAL258
B	LYS265
B	PHE266
B	HIS267
B	ASP280
B	HOH1211

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 806

Chain	Residue
B	HIS218
B	LYS219
B	HOH1901

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 807

Chain	Residue
B	TYR160
B	LEU558
B	LYS561
B	SER591
B	HOH1484
B	HOH1712
C	LYS561
C	ASP593
C	GOL809
C	HOH1147

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 808

Chain	Residue
B	GLY142
B	PRO144
B	GLU147
B	TYR177
B	HOH1327
D	HOH1360

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 809

Chain	Residue
B	PHE310
B	HOH1069
B	HOH1162
B	HOH1281
B	HOH1395
B	HOH1792
B	HOH1840
C	GLY594
C	HOH1160

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO C 801

Chain	Residue
C	TYR405
C	HIS456
C	HIS458
C	HIS624
C	HOH1633
C	HOH1731

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 802

Chain	Residue
C	ARG213
C	LYS214
C	VAL215
C	GLY435
C	ASP436
C	HOH1076
C	HOH1170

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 803

Chain	Residue
C	GLU368
C	LYS393
C	TYR410
C	VAL412
C	ARG420
C	ASP422
C	HOH1047
C	HOH1767
D	GLY371

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 804

Chain	Residue
C	HIS218
C	LYS219
C	HOH1497
C	HOH1608

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 805

Chain	Residue
C	PRO484
C	TYR485
C	TYR499
C	HOH1395
C	HOH1662
D	PRO442
D	TRP443

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 806

Chain	Residue
C	HIS23
C	TYR64
C	LYS68
C	LYS265
C	ASP280
C	HOH1067
C	HOH1578
C	HOH1586

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 807

Chain	Residue
B	GLN66
B	GLN70
B	GLY72
C	TYR534
C	THR650
C	HOH1032
C	HOH1265

site_id	DC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 808

Chain	Residue
B	GLY594
B	HOH1154
C	ARG163
C	PHE310
C	HOH1113
C	HOH1181
C	HOH1274
C	HOH1367
C	HOH1837

site_id	DC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 809

Chain	Residue
B	LYS561
B	ASP593
B	GOL807
C	LEU558
C	LYS561
C	SER591
C	HOH1147
C	HOH1668

site_id	DC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 810

Chain	Residue
B	TRP67
B	LYS68

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO D 801

Chain	Residue
D	TYR405
D	HIS456
D	HIS458
D	HIS624
D	HOH1642
D	HOH1745

site_id	DC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 802

Chain	Residue
D	HIS23
D	TYR64
D	LYS68
D	LYS265
D	ASP280
D	HOH1167
D	HOH1870

site_id	DC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL D 803

Chain	Residue
D	GLU368
D	LYS393
D	TYR410
D	VAL412
D	ARG420
D	ASP422
D	ARG424
D	HOH1051
D	HOH1596
D	HOH1772
D	HOH1934

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 804

Chain	Residue
D	PRO484
D	TYR485
D	TYR499
D	HOH1586
D	HOH1643

site_id	DC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 805

Chain	Residue
D	SER179
D	ASP183
D	HIS188
D	HIS218
D	LYS219
D	HIS220
D	HOH1313
D	HOH1550

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 806

Chain	Residue
B	HOH1152
B	HOH1742
C	HOH1101
D	HIS218
D	LYS219
D	TYR448

site_id	EC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO E 801

Chain	Residue
E	TYR405
E	HIS456
E	HIS458
E	HIS624
E	HOH1637
E	HOH1731

site_id	EC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 802

Chain	Residue
E	HIS23
E	TYR64
E	LYS68
E	LYS265
E	ASP280
E	HOH1225
E	HOH1368
E	HOH1756

site_id	EC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL E 803

Chain	Residue
E	GLU368
E	LYS393
E	TYR410
E	VAL412
E	ARG420
E	ASP422
E	ARG424
E	HOH922
E	HOH1620
F	GLY371

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 804

Chain	Residue
E	PRO484
E	TYR485
E	HOH1658
E	HOH1852

site_id	EC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL E 805

Chain	Residue
A	ASN529
A	HOH1892
E	LYS214
E	VAL215
E	ASP436
E	ASN450
E	HOH1050
E	HOH1151
E	HOH1326

site_id	EC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 806

Chain	Residue
A	HOH1571
A	HOH1688
E	HIS218
E	LYS219
E	TYR448
F	HOH1037

site_id	EC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CO F 801

Chain	Residue
F	TYR405
F	LEU425
F	HIS456
F	HIS458
F	HIS624
F	HOH1599
F	HOH1705

site_id	EC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 802

Chain	Residue
F	HIS23
F	TYR64
F	LYS68
F	LYS265
F	ASP280
F	HOH1093
F	HOH1490

site_id	EC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 803

Chain	Residue
F	ARG213
F	LYS214
F	VAL215
F	GLY435
F	ASP436
F	HOH1095
F	HOH1725

site_id	FC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GOL F 804

Chain	Residue
E	GLY371
F	GLU368
F	LYS393
F	TYR410
F	VAL412
F	ARG420
F	ASP422
F	ARG424
F	HOH1059
F	HOH1133
F	HOH1634
F	HOH1696
F	HOH1703
F	HOH1896

site_id	FC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 805

Chain	Residue
E	PRO442
F	PRO484
F	TYR485
F	TYR499
F	HOH1181
F	HOH1527

site_id	FC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 806

Chain	Residue
F	HIS218
F	LYS219
F	HOH1675
F	HOH1887

site_id	FC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL F 807

Chain	Residue
A	TRP67
A	LYS68

site_id	FC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL F 808

Chain	Residue
A	LYS561
A	ASP593
A	GOL810
F	TYR160
F	LEU558
F	LYS561
F	SER591
F	HOH1087
F	HOH1623

site_id	FC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL F 809

Chain	Residue
A	GLY594
A	HOH952
F	ARG163
F	PHE310
F	HOH934
F	HOH1190
F	HOH1204
F	HOH1313
F	HOH1857

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	30
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P46883","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
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)