Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OQE

Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 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 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
D	0005507	molecular_function	copper ion binding
D	0005777	cellular_component	peroxisome
D	0008131	molecular_function	primary amine oxidase activity
D	0009308	biological_process	amine metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0048038	molecular_function	quinone binding
D	0052595	molecular_function	aliphatic amine oxidase activity
E	0005507	molecular_function	copper ion binding
E	0005777	cellular_component	peroxisome
E	0008131	molecular_function	primary amine oxidase activity
E	0009308	biological_process	amine metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0048038	molecular_function	quinone binding
E	0052595	molecular_function	aliphatic amine oxidase activity
F	0005507	molecular_function	copper ion binding
F	0005777	cellular_component	peroxisome
F	0008131	molecular_function	primary amine oxidase activity
F	0009308	biological_process	amine metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0048038	molecular_function	quinone binding
F	0052595	molecular_function	aliphatic amine oxidase activity

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:9551552

Chain	Residue	Details
C	ASP319
D	ASP319
E	ASP319
F	ASP319

site_id	SWS_FT_FI2
Number of Residues	4
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
C	TPQ405
D	TPQ405
E	TPQ405
F	TPQ405

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

Chain	Residue	Details
C	ALA317
D	ALA317
E	ALA317
F	ALA317

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P46883

Chain	Residue	Details
C	ALA402
D	ALA402
E	ALA402
F	ALA402

site_id	SWS_FT_FI5
Number of Residues	12
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
C	HIS456
F	HIS456
F	HIS458
F	HIS624
C	HIS458
C	HIS624
D	HIS456
D	HIS458
D	HIS624
E	HIS456
E	HIS458
E	HIS624

site_id	SWS_FT_FI6
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q43077

Chain	Residue	Details
C	ASP465
F	ASP465
F	ASP613
F	ILE614
C	ASP613
C	ILE614
D	ASP465
D	ASP613
D	ILE614
E	ASP465
E	ASP613
E	ILE614

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

Chain	Residue	Details
C	TPQ405
D	TPQ405
E	TPQ405
F	TPQ405

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:9551552

Chain	Residue	Details
C	ASN243
D	ASN243
E	ASN243
F	ASN243

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