Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OOV

Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms

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	4
Details	BINDING SITE FOR RESIDUE CU A 801

Chain	Residue
A	HIS456
A	HIS458
A	HIS624
A	HOH6215

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 801

Chain	Residue
B	HIS456
B	HIS458
B	HIS624
B	HOH6210

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 801

Chain	Residue
C	HIS456
C	HIS458
C	HIS624
C	TPQ405

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU D 801

Chain	Residue
D	TPQ405
D	LEU425
D	HIS456
D	HIS458
D	HIS624
D	HOH6751

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU E 801

Chain	Residue
E	TPQ405
E	HIS456
E	HIS458
E	HIS624
E	HOH6752

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU F 801

Chain	Residue
F	TPQ405
F	HIS456
F	HIS458
F	HIS624

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 6010

Chain	Residue
C	HIS218
C	LYS219
C	HOH6697
C	HOH6762
C	HOH6767

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 6011

Chain	Residue
F	HIS218
F	LYS219
F	HOH6701
F	HOH6717

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 6001

Chain	Residue
F	HIS23
F	TYR64
F	LYS68
F	LYS265
F	ASP280
F	HOH6166
F	HOH6746

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 6002

Chain	Residue
C	LYS214
C	VAL215
C	ASP436
C	HOH6215
C	HOH6429
C	HOH6812

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL F 6003

Chain	Residue
F	PHE51
F	ASN52
F	THR117
F	GLU119
F	ASP120
F	TYR327
F	SER350
F	ASP351
F	ARG352
F	HOH6198

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 6004

Chain	Residue
B	ARG213
B	LYS214
B	VAL215
B	ASP436
B	ASN450
B	HOH6581
B	HOH6758

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 6005

Chain	Residue
A	LYS214
A	VAL215
A	ASP436
A	HOH6370

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL F 6006

Chain	Residue
F	LYS214
F	VAL215
F	GLY435
F	ASP436
F	HOH6453

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 6007

Chain	Residue
C	LYS393
C	VAL412
C	ASP422
C	ARG424
C	HOH6164
C	HOH6785
C	HOH6873

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 6008

Chain	Residue
E	GLY371
F	LYS393
F	ASP422
F	ARG424
F	HOH6112
F	HOH6644
F	HOH6687

site_id	BC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 6009

Chain	Residue
B	HOH6774
A	GLY371
B	GLU368
B	LYS393
B	TYR410
B	ARG420
B	ASP422
B	ARG424
B	HOH6156
B	HOH6507
B	HOH6677

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 6012

Chain	Residue
A	GLU368
A	LYS393
A	VAL412
A	ARG420
A	ASP422
A	HOH6118
A	HOH6557
A	HOH6789
B	GLY371

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 6013

Chain	Residue
A	ARG61
A	LYS62
A	ASP471
A	ASP613
A	HOH6623
A	HOH6707

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 6014

Chain	Residue
E	LYS214
E	VAL215
E	ASP436
E	HOH6235
E	HOH6791
E	HOH6792
E	HOH6793

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 6015

Chain	Residue
A	ASP471
A	HOH6707
E	HIS218
E	LYS219
E	TYR448
E	HOH6415

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 6016

Chain	Residue
E	PRO442
E	TRP443
F	PRO484
F	TYR499

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 6017

Chain	Residue
A	ARG163
A	PHE310
A	HOH6315
A	HOH6442
A	HOH6632
A	HOH6844
B	HOH6144
F	ASP593
F	GLY594

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 6018

Chain	Residue
A	HIS218
A	LYS219
A	TYR448
A	HOH6471

site_id	CC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL E 6019

Chain	Residue
E	LYS393
E	VAL412
E	ARG420
E	ASP422
E	ARG424
E	HOH6067
E	HOH6621
E	HOH6664
E	HOH6713
F	GLY371

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL E 6020

Chain	Residue
E	PRO484
F	PRO442

site_id	CC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 6021

Chain	Residue
C	HIS286
C	PHE649
C	THR650
C	GLU651
C	PRO653
C	GOL6029
C	HOH6125
C	HOH6181
C	HOH6294
C	HOH6530

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 6022

Chain	Residue
E	ILE208
E	PRO209
E	ASN210
E	PHE310
E	HOH6131
E	HOH6282
E	HOH6674

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 6023

Chain	Residue
B	GLY142
B	PRO144
B	GLU147
B	TYR177
B	HOH6704
D	HOH6484

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 6024

Chain	Residue
B	PRO484
B	TYR499
B	HOH6808

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 6025

Chain	Residue
B	GLY603
B	ASP604
B	HOH6375
B	HOH6599
D	PRO490
D	GLU491

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 6026

Chain	Residue
B	HIS218
B	LYS219
B	TYR448
B	HOH6275
B	HOH6757

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 6027

Chain	Residue
A	PRO484
A	TYR485
A	TYR499
A	HOH6829
A	HOH6862
B	PRO442

site_id	DC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 6028

Chain	Residue
D	ARG20
D	PRO21
D	LEU74
D	PRO75
D	ARG77
D	HOH6304
D	HOH6372
D	HOH6662
D	HOH6867

site_id	DC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 6029

Chain	Residue
B	GLN66
B	GLN70
B	GLY72
C	TYR534
C	THR650
C	GLU651
C	GOL6021
C	HOH6076
C	HOH6530
D	TYR448

site_id	DC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 6030

Chain	Residue
C	GLY371
D	LYS393
D	VAL412
D	ARG420
D	ASP422
D	ARG424
D	HOH6088
D	HOH6516
D	HOH6744
D	HOH6769

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
C	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
C	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
C	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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
A	ASP319

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
B	ASP319

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
C	ASP319

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
D	ASP319

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
E	ASP319

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1oac

Chain	Residue	Details
F	ASP319

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